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amyloid precursor protein-cleaving enzyme 1</title> <meta name="description" content="Search results for: β-site amyloid precursor protein-cleaving enzyme 1"> <meta name="keywords" content="β-site amyloid precursor protein-cleaving enzyme 1"> <meta name="viewport" content="width=device-width, initial-scale=1, minimum-scale=1, maximum-scale=1, user-scalable=no"> <meta charset="utf-8"> <link href="https://cdn.waset.org/favicon.ico" type="image/x-icon" rel="shortcut icon"> <link href="https://cdn.waset.org/static/plugins/bootstrap-4.2.1/css/bootstrap.min.css" rel="stylesheet"> <link href="https://cdn.waset.org/static/plugins/fontawesome/css/all.min.css" rel="stylesheet"> <link href="https://cdn.waset.org/static/css/site.css?v=150220211555" rel="stylesheet"> </head> <body> <header> <div class="container"> <nav class="navbar navbar-expand-lg navbar-light"> <a class="navbar-brand" href="https://waset.org"> <img src="https://cdn.waset.org/static/images/wasetc.png" alt="Open Science Research 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</div> </div> <h1 class="mt-3 mb-3 text-center" style="font-size:1.6rem;">Search results for: β-site amyloid precursor protein-cleaving enzyme 1</h1> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">1259</span> The Effect of Dendrobium nobile Lindl. Alkaloids on the Blood Glucose and Amyloid Precursor Protein Metabolic Pathways in Db/Db Mice</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Juan%20Huang">Juan Huang</a>, <a href="https://publications.waset.org/abstracts/search?q=Nanqu%20Huang"> Nanqu Huang</a>, <a href="https://publications.waset.org/abstracts/search?q=Jingshan%20Shi"> Jingshan Shi</a>, <a href="https://publications.waset.org/abstracts/search?q=Yu%20Qiu"> Yu Qiu</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Objectives: There are pathophysiological connections between type 2 diabetes mellitus (T2DM) and Alzheimer's disease (AD), and research on drugs with hypoglycemic and beta-amyloid (Aβ)-clearing effects have great therapeutic potential for AD. Dendrobium nobile Lindl. Alkaloids (DNLA) as one of the active compounds of Dendrobium nobile Lindl. In this study, we attempted to verify the hypoglycemic effect and investigate the effects of DNLA on the amyloid precursor protein (APP) metabolic pathway of the hippocampus in db/db mice. Methods: 4-weeks-old male C57BL/KsJ mice were the control group. And the same age and sexuality db/db mice were: model, DNLA-L (20 mg/kg), DNLA-M (40 mg/kg), and DNLA-H (80 mg/kg). After, mice were treated with different concentrations of DNLA for 17 weeks. The fasting blood glucose (FBG) was detected by glucose oxidase assay every week from the 4th to last week. The protein expression of β-amyloid 1-42 (Aβ1-42), β-site amyloid precursor protein-cleaving enzyme 1 (BACE1), and APP were examined by Western blotting. Results: The concentration of FBG and the protein expression of Aβ1-42, BACE1, and APP were increased in the hippocampus of the model group. Moreover, DNLA not only significantly decreased the concentration of FBG but also reduced the protein expressions of Aβ1-42, BACE1 and APP in the hippocampus of db/db mice in a dose-dependent manner. Conclusions: DNLA can decrease the protein expressions of Aβ1-42 in the hippocampus of db/db mice, and the mechanism may be involved in the APP metabolic pathway. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=Alzheimer%27s%20disease" title="Alzheimer's disease">Alzheimer's disease</a>, <a href="https://publications.waset.org/abstracts/search?q=type%202%20diabetes%20mellitus" title=" type 2 diabetes mellitus"> type 2 diabetes mellitus</a>, <a href="https://publications.waset.org/abstracts/search?q=%CE%B2-site%20amyloid%20precursor%20protein-cleaving%20enzyme%201" title=" β-site amyloid precursor protein-cleaving enzyme 1"> β-site amyloid precursor protein-cleaving enzyme 1</a>, <a href="https://publications.waset.org/abstracts/search?q=traditional%20Chinese%20medicines" title=" traditional Chinese medicines"> traditional Chinese medicines</a>, <a href="https://publications.waset.org/abstracts/search?q=beta-amyloid" title=" beta-amyloid"> beta-amyloid</a> </p> <a href="https://publications.waset.org/abstracts/152548/the-effect-of-dendrobium-nobile-lindl-alkaloids-on-the-blood-glucose-and-amyloid-precursor-protein-metabolic-pathways-in-dbdb-mice" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/152548.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">255</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">1258</span> Structure-Guided Optimization of Sulphonamide as Gamma–Secretase Inhibitors for the Treatment of Alzheimer’s Disease</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Vaishali%20Patil">Vaishali Patil</a>, <a href="https://publications.waset.org/abstracts/search?q=Neeraj%20Masand"> Neeraj Masand</a> </p> <p class="card-text"><strong>Abstract:</strong></p> In older people, Alzheimer’s disease (AD) is turning out to be a lethal disease. According to the amyloid hypothesis, aggregation of the amyloid β–protein (Aβ), particularly its 42-residue variant (Aβ42), plays direct role in the pathogenesis of AD. Aβ is generated through sequential cleavage of amyloid precursor protein (APP) by β–secretase (BACE) and γ–secretase (GS). Thus in the treatment of AD, γ-secretase modulators (GSMs) are potential disease-modifying as they selectively lower pathogenic Aβ42 levels by shifting the enzyme cleavage sites without inhibiting γ–secretase activity. This possibly avoids known adverse effects observed with complete inhibition of the enzyme complex. Virtual screening, via drug-like ADMET filter, QSAR and molecular docking analyses, has been utilized to identify novel γ–secretase modulators with sulphonamide nucleus. Based on QSAR analyses and docking score, some novel analogs have been synthesized. The results obtained by in silico studies have been validated by performing in vivo analysis. In the first step, behavioral assessment has been carried out using Scopolamine induced amnesia methodology. Later the same series has been evaluated for neuroprotective potential against the oxidative stress induced by Scopolamine. Biochemical estimation was performed to evaluate the changes in biochemical markers of Alzheimer’s disease such as lipid peroxidation (LPO), Glutathione reductase (GSH), and Catalase. The Scopolamine induced amnesia model has shown increased Acetylcholinesterase (AChE) levels and the inhibitory effect of test compounds in the brain AChE levels have been evaluated. In all the studies Donapezil (Dose: 50µg/kg) has been used as reference drug. The reduced AChE activity is shown by compounds 3f, 3c, and 3e. In the later stage, the most potent compounds have been evaluated for Aβ42 inhibitory profile. It can be hypothesized that this series of alkyl-aryl sulphonamides exhibit anti-AD activity by inhibition of Acetylcholinesterase (AChE) enzyme as well as inhibition of plaque formation on prolong dosage along with neuroprotection from oxidative stress. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=gamma-secretase%20inhibitors" title="gamma-secretase inhibitors">gamma-secretase inhibitors</a>, <a href="https://publications.waset.org/abstracts/search?q=Alzzheimer%27s%20disease" title=" Alzzheimer's disease"> Alzzheimer's disease</a>, <a href="https://publications.waset.org/abstracts/search?q=sulphonamides" title=" sulphonamides"> sulphonamides</a>, <a href="https://publications.waset.org/abstracts/search?q=QSAR" title=" QSAR"> QSAR</a> </p> <a href="https://publications.waset.org/abstracts/77906/structure-guided-optimization-of-sulphonamide-as-gamma-secretase-inhibitors-for-the-treatment-of-alzheimers-disease" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/77906.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">255</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">1257</span> Amyloid Deposition in Granuloma of Tuberculosis Patients: A Pilot Study</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Shreya%20Ghosh">Shreya Ghosh</a>, <a href="https://publications.waset.org/abstracts/search?q=Akansha%20Garg"> Akansha Garg</a>, <a href="https://publications.waset.org/abstracts/search?q=Chayanika%20Kala"> Chayanika Kala</a>, <a href="https://publications.waset.org/abstracts/search?q=Ashwani%20Kumar%20Thakur"> Ashwani Kumar Thakur</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Background: Granuloma formation is one of the characteristic features of tuberculosis. Besides, chronic inflammation underlying tuberculosis is often indicated by an increase in the concentration of serum amyloid A (SAA) protein. The connection between tuberculosis and SAA-driven secondary amyloidosis is well documented. However, SAA-derived amyloid deposition start sites are not well understood in tuberculosis and other chronic inflammatory conditions. It was hypothesized that granuloma could be a potential site for an amyloid deposition because both SAA protein and proteases that cleave SAA into aggregation-prone fragments are reported to be present in the granuloma. Here the authors have shown the presence of SAA-derived amyloid deposits in the granuloma of tuberculosis patients. Methodology: Over a period of two years, tuberculosis patients were screened, and biopsies were collected from the affected organs of the patients. The gold standard, Congo red dye staining, was used to identify amyloid deposits in the tissue sections of tuberculosis patients containing granulomatous structure. Results: 11 out of 150 FFPE biopsy specimens of tuberculosis patients showed eosinophilic hyaline-rich deposits surrounding granuloma. Upon Congo red staining, these deposits exhibited characteristic apple-green birefringence under polarized light, confirming amyloid deposits. Further, upon immunohistochemical staining with anti-SAA, the amyloid enriched areas showed positive immunoreactivity. Conclusion: In this pilot study, we have shown that granuloma can be a potential site for serum amyloid A-derived amyloid formation in tuberculosis patients. Moreover, the presence of amyloid gave significant cues that granuloma might be a probable amyloid deposition start in tuberculosis patients. This study will set a stage to expand the clinical and fundamental research in the understanding of amyloid formation in granuloma underlying tuberculosis and chronic inflammatory conditions. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=amyloid" title="amyloid">amyloid</a>, <a href="https://publications.waset.org/abstracts/search?q=granuloma" title=" granuloma"> granuloma</a>, <a href="https://publications.waset.org/abstracts/search?q=periphery" title=" periphery"> periphery</a>, <a href="https://publications.waset.org/abstracts/search?q=serum%20amyloid%20A" title=" serum amyloid A"> serum amyloid A</a>, <a href="https://publications.waset.org/abstracts/search?q=tuberculosis" title=" tuberculosis"> tuberculosis</a> </p> <a href="https://publications.waset.org/abstracts/136557/amyloid-deposition-in-granuloma-of-tuberculosis-patients-a-pilot-study" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/136557.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">195</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">1256</span> Targeting APP IRE mRNA to Combat Amyloid -β Protein Expression in Alzheimer’s Disease</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Mateen%20A%20Khan">Mateen A Khan</a>, <a href="https://publications.waset.org/abstracts/search?q=Taj%20Mohammad"> Taj Mohammad</a>, <a href="https://publications.waset.org/abstracts/search?q=Md.%20Imtaiyaz%20Hassan"> Md. Imtaiyaz Hassan</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Alzheimer’s disease is characterized by the accumulation of the processing products of the amyloid beta peptide cleaved by amyloid precursor protein (APP). Iron increases the synthesis of amyloid beta peptides, which is why iron is present in Alzheimer's disease patients' amyloid plaques. Iron misregulation in the brain is linked to the overexpression of APP protein, which is directly related to amyloid-β aggregation in Alzheimer’s disease. The APP 5'-UTR region encodes a functional iron-responsive element (IRE) stem-loop that represents a potential target for modulating amyloid production. Targeted regulation of APP gene expression through the modulation of 5’-UTR sequence function represents a novel approach for the potential treatment of AD because altering APP translation can be used to improve both the protective brain iron balance and provide anti-amyloid efficacy. The molecular docking analysis of APP IRE RNA with eukaryotic translation initiation factors yields several models exhibiting substantial binding affinity. The finding revealed that the interaction involved a set of functionally active residues within the binding sites of eIF4F. Notably, APP IRE RNA and eIF4F interaction were stabilized by multiple hydrogen bonds with residues of APP IRE RNA and eIF4F. It was evident that APP IRE RNA exhibited a structural complementarity that tightly fit within binding pockets of eIF4F. The simulation studies further revealed the stability of the complexes formed between RNA and eIF4F, which is crucial for assessing the strength of these interactions and subsequent roles in the pathophysiology of Alzheimer’s disease. In addition, MD simulations would capture conformational changes in the IRE RNA and protein molecules during their interactions, illustrating the mechanism of interaction, conformational change, and unbinding events and how it may affect aggregation propensity and subsequent therapeutic implications. Our binding studies correlated well with the translation efficiency of APP mRNA. Overall, the outcome of this study suggests that the genomic modification and/or inhibiting the expression of amyloid protein by targeting APP IRE RNA can be a viable strategy to identify potential therapeutic targets for AD and subsequently be exploited for developing novel therapeutic approaches. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=Alzheimer%27s%20disease" title="Alzheimer's disease">Alzheimer's disease</a>, <a href="https://publications.waset.org/abstracts/search?q=Protein-RNA%20interaction%20analysis" title=" Protein-RNA interaction analysis"> Protein-RNA interaction analysis</a>, <a href="https://publications.waset.org/abstracts/search?q=molecular%20docking%20simulations" title=" molecular docking simulations"> molecular docking simulations</a>, <a href="https://publications.waset.org/abstracts/search?q=conformational%20dynamics" title=" conformational dynamics"> conformational dynamics</a>, <a href="https://publications.waset.org/abstracts/search?q=binding%20stability" title=" binding stability"> binding stability</a>, <a href="https://publications.waset.org/abstracts/search?q=binding%20kinetics" title=" binding kinetics"> binding kinetics</a>, <a href="https://publications.waset.org/abstracts/search?q=protein%20synthesis." title=" protein synthesis."> protein synthesis.</a> </p> <a href="https://publications.waset.org/abstracts/186190/targeting-app-ire-mrna-to-combat-amyloid-v-protein-expression-in-alzheimers-disease" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/186190.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">64</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">1255</span> Potential of Polyphenols from Tamarix Gallica towards Common Pathological Features of Diabetes and Alzheimer’s Diseases</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Asma%20Ben%20Hmidene">Asma Ben Hmidene</a>, <a href="https://publications.waset.org/abstracts/search?q=Mizuho%20Hanaki"> Mizuho Hanaki</a>, <a href="https://publications.waset.org/abstracts/search?q=Kazuma%20Murakami"> Kazuma Murakami</a>, <a href="https://publications.waset.org/abstracts/search?q=Kazuhiro%20Irie"> Kazuhiro Irie</a>, <a href="https://publications.waset.org/abstracts/search?q=Hiroko%20Isoda"> Hiroko Isoda</a>, <a href="https://publications.waset.org/abstracts/search?q=Hideyuki%20Shigemori"> Hideyuki Shigemori</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Type 2 diabetes mellitus (T2DM) and Alzheimer’s disease (AD) are characterized as a peripheral metabolic disorder and a degenerative disease of the central nervous system, respectively. It is now widely recognized that T2DM and AD share many pathophysiological features including glucose metabolism, increased oxidative stress and amyloid aggregation. Amyloid beta (Aβ) is the components of the amyloid deposits in the AD brain and while the component of the amyloidogenic peptide deposit in the pancreatic islets of Langerhans is identified as human islet amyloid polypeptide (hIAPP). These two proteins are originated from the amyloid precursor protein and have a high sequence similarity. Although the amino acid sequences of amyloidogenic proteins are diverse, they all adopt a similar structure in aggregates called cross-beta-spine. Add at that, extensive studies in the past years have found that like Aβ1-42, IAPP forms early intermediate assemblies as spherical oligomers, implicating that these oligomers possess a common folding pattern or conformation. These similarities can be used in the search for effective pharmacotherapy for DM, since potent therapeutic agents such as antioxidants with a catechol moiety, proved to inhibit Aβ aggregation, may play a key role in the inhibit the aggregation of hIAPP treatment of patients with DM. Tamarix gallica is one of the halophyte species having a powerful antioxidant system. Although it was traditionally used for the treatment of various liver metabolic disorders, there is no report about the use of this plant for the treatment or prevention of T2DM and AD. Therefore, the aim of this work is to investigate their protective effect towards T2DM and AD by isolation and identification of α-glucosidase inhibitors, with antioxidant potential, that play an important role in the glucose metabolism in diabetic patient, as well as, the polymerization of hIAPP and Aβ aggregation inhibitors. Structure-activity relationship study was conducted for both assays. And as for α-glucosidase inhibitors, their mechanism of action and their synergistic potential when applied with a very low concentration of acarbose were also suggesting that they can be used not only as α-glucosidase inhibitors but also be combined with established α-glucosidase inhibitors to reduce their adverse effect. The antioxidant potential of the purified substances was evaluated by DPPH and SOD assays. Th-T assay using 42-mer amyloid β-protein (Aβ42) for AD and hIAPP which is a 37-residue peptide secreted by the pancreatic β –cells for T2DM and Transmission electronic microscopy (TEM) were conducted to evaluate the amyloid aggragation of the actives substances. For α-glucosidase, p-NPG and glucose oxidase assays were performed for determining the inhibition potential and structure-activity relationship study. The Enzyme kinetic protocol was used to study the mechanism of action. From this research, it was concluded that polyphenols playing a role in the glucose metabolism and oxidative stress can also inhibit the amyloid aggregation, and that substances with a catechol and glucuronide moieties inhibiting amyloid-β aggregation, might be used to inhibit the aggregation of hIAPP. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=%CE%B1-glucosidase%20inhibitors" title="α-glucosidase inhibitors">α-glucosidase inhibitors</a>, <a href="https://publications.waset.org/abstracts/search?q=amyloid%20aggregation%20inhibition" title=" amyloid aggregation inhibition"> amyloid aggregation inhibition</a>, <a href="https://publications.waset.org/abstracts/search?q=mechanism%20of%20action" title=" mechanism of action"> mechanism of action</a>, <a href="https://publications.waset.org/abstracts/search?q=polyphenols" title=" polyphenols"> polyphenols</a>, <a href="https://publications.waset.org/abstracts/search?q=structure%20activity%20relationship" title=" structure activity relationship"> structure activity relationship</a>, <a href="https://publications.waset.org/abstracts/search?q=synergistic%20potential" title=" synergistic potential"> synergistic potential</a>, <a href="https://publications.waset.org/abstracts/search?q=tamarix%20gallica" title=" tamarix gallica"> tamarix gallica</a> </p> <a href="https://publications.waset.org/abstracts/56581/potential-of-polyphenols-from-tamarix-gallica-towards-common-pathological-features-of-diabetes-and-alzheimers-diseases" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/56581.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">279</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">1254</span> Molecular Basis for Amyloid Inhibition by L-Dopa: Implication towards Systemic Amyloidosis</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Rizwan%20H.%20Khan">Rizwan H. Khan</a>, <a href="https://publications.waset.org/abstracts/search?q=Saima%20Nusrat"> Saima Nusrat</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Despite the fact that amyloid associated neurodegenerative diseases and non-neuropathic systemic amyloidosis have allured the research endeavors, as no curative drugs have been proclaimed up till now except for symptomatic cure. Therapeutic compounds which can diminish or disaggregate such toxic oligomers and fibrillar species have been examined and more are on its way. In the present study, we had reported an extensive biophysical, microscopic and computational study, revealing that L-3, 4-dihydroxyphenylalanine (L-Dopa) possess undeniable potency to inhibit heat induced human lysozyme (HL) amyloid fibrillation and also retain the fibril disaggregating potential. L-Dopa interferes in the amyloid fibrillogenesis process by interacting hydrophobically and also by forming hydrogen bonds with the amino acid residues found in amyloid fibril forming prone region of HL as elucidated by molecular docking results. L-Dopa also disaggregates the mature amyloid fibrils into some unorganised species. Thus, L-Dopa and related compounds can work as a promising inhibitor for the therapeutic advancement prospective against systemic amyloidosis. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=amyloids" title="amyloids">amyloids</a>, <a href="https://publications.waset.org/abstracts/search?q=disaggregation" title=" disaggregation"> disaggregation</a>, <a href="https://publications.waset.org/abstracts/search?q=human%20lysozyme" title=" human lysozyme"> human lysozyme</a>, <a href="https://publications.waset.org/abstracts/search?q=molecular%20docking" title=" molecular docking"> molecular docking</a> </p> <a href="https://publications.waset.org/abstracts/67120/molecular-basis-for-amyloid-inhibition-by-l-dopa-implication-towards-systemic-amyloidosis" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/67120.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">327</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">1253</span> Inhibitory Impacts of Fulvic Acid-Coated Iron Oxide Nano Particles on the Amyloid Fibril Aggregations</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Dalia%20Jomehpour">Dalia Jomehpour</a>, <a href="https://publications.waset.org/abstracts/search?q=Sara%20Sheikhlary"> Sara Sheikhlary</a>, <a href="https://publications.waset.org/abstracts/search?q=Esmaeil%20Heydari"> Esmaeil Heydari</a>, <a href="https://publications.waset.org/abstracts/search?q=Mohammad%20Hossien%20Majles%20Ara"> Mohammad Hossien Majles Ara</a> </p> <p class="card-text"><strong>Abstract:</strong></p> In this study, we report fulvic acid-coated iron oxide nanoparticles of 10.7 ± 2.7 nm size, which serve to inhibit amyloid fibrillation formation. Although the effect of fulvic acid on tau fibrils was investigated, to our best knowledge, its inhibitory impacts on amyloid aggregation formation have been assessed neither in-vitro nor in-vivo. On the other hand, iron oxide nanoparticles exhibit anti-amyloid activity on their own. This study investigates the inhibitory effect of fulvic acid coated iron oxide nanoparticles on amyloid aggregations formed from the commonly used in-vitro model, lysozyme from chicken egg white. FESEM, XRD, and FTIR characterization confirmed that fulvic acid was coated onto the surface of the nanoparticles. The inhibitory effects of the fulvic acid coated iron oxide nanoparticles were verified by Thioflavin T assay, circular dichroism (CD), and FESEM analysis. Furthermore, the toxicity of the nanoparticles on the neuroblastoma SH-SY5Y human cell line was assessed through an MTT assay. Our results indicate that fulvic acid coated iron oxide nanoparticles can efficiently inhibit the formation of amyloid aggregations while exhibiting negligible in-vitro toxicity; thus, they can be used as anti-amyloid agents in the development of the potential drug for neurodegenerative diseases. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=Alzheimer%E2%80%99s%20disease" title="Alzheimer’s disease">Alzheimer’s disease</a>, <a href="https://publications.waset.org/abstracts/search?q=fulvic%20acid%20coated%20iron%20oxide%20nanoparticles" title=" fulvic acid coated iron oxide nanoparticles"> fulvic acid coated iron oxide nanoparticles</a>, <a href="https://publications.waset.org/abstracts/search?q=fulvic%20acid" title=" fulvic acid"> fulvic acid</a>, <a href="https://publications.waset.org/abstracts/search?q=amyloid%20inhibitor" title=" amyloid inhibitor"> amyloid inhibitor</a>, <a href="https://publications.waset.org/abstracts/search?q=polyphenols" title=" polyphenols"> polyphenols</a> </p> <a href="https://publications.waset.org/abstracts/152105/inhibitory-impacts-of-fulvic-acid-coated-iron-oxide-nano-particles-on-the-amyloid-fibril-aggregations" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/152105.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">112</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">1252</span> Amyloid-β Fibrils Remodeling by an Organic Molecule: Insight from All-Atomic Molecular Dynamics Simulations</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Nikhil%20Agrawal">Nikhil Agrawal</a>, <a href="https://publications.waset.org/abstracts/search?q=Adam%20A.%20Skelton"> Adam A. Skelton</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Alzheimer’s disease (AD) is one of the most common forms of dementia, which is caused by misfolding and aggregation of amyloid beta (Aβ) peptides into amyloid-β fibrils (Aβ fibrils). To disrupt the remodeling of Aβ fibrils, a number of candidate molecules have been proposed. To study the molecular mechanisms of Aβ fibrils remodeling we performed a series of all-atom molecular dynamics simulations, a total time of 3µs, in explicit solvent. Several previously undiscovered candidate molecule-Aβ fibrils binding modes are unraveled; one of which shows the direct conformational change of the Aβ fibril by understanding the physicochemical factors responsible for binding and subsequent remodeling of Aβ fibrils by the candidate molecule, open avenues into structure-based drug design for AD can be opened. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=alzheimer%E2%80%99s%20disease" title="alzheimer’s disease">alzheimer’s disease</a>, <a href="https://publications.waset.org/abstracts/search?q=amyloid" title=" amyloid"> amyloid</a>, <a href="https://publications.waset.org/abstracts/search?q=MD%20simulations" title=" MD simulations"> MD simulations</a>, <a href="https://publications.waset.org/abstracts/search?q=misfolded%20protein" title=" misfolded protein"> misfolded protein</a> </p> <a href="https://publications.waset.org/abstracts/52879/amyloid-v-fibrils-remodeling-by-an-organic-molecule-insight-from-all-atomic-molecular-dynamics-simulations" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/52879.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">347</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">1251</span> A Computational Investigation of Potential Drugs for Cholesterol Regulation to Treat Alzheimer’s Disease</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Marina%20Passero">Marina Passero</a>, <a href="https://publications.waset.org/abstracts/search?q=Tianhua%20Zhai"> Tianhua Zhai</a>, <a href="https://publications.waset.org/abstracts/search?q=Zuyi%20%28Jacky%29%20Huang"> Zuyi (Jacky) Huang</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Alzheimer’s disease has become a major public health issue, as indicated by the increasing populations of Americans living with Alzheimer’s disease. After decades of extensive research in Alzheimer’s disease, only seven drugs have been approved by Food and Drug Administration (FDA) to treat Alzheimer’s disease. Five of these drugs were designed to treat the dementia symptoms, and only two drugs (i.e., Aducanumab and Lecanemab) target the progression of Alzheimer’s disease, especially the accumulation of amyloid-b plaques. However, controversial comments were raised for the accelerated approvals of either Aducanumab or Lecanemab, especially with concerns on safety and side effects of these two drugs. There is still an urgent need for further drug discovery to target the biological processes involved in the progression of Alzheimer’s disease. Excessive cholesterol has been found to accumulate in the brain of those with Alzheimer’s disease. Cholesterol can be synthesized in both the blood and the brain, but the majority of biosynthesis in the adult brain takes place in astrocytes and is then transported to the neurons via ApoE. The blood brain barrier separates cholesterol metabolism in the brain from the rest of the body. Various proteins contribute to the metabolism of cholesterol in the brain, which offer potential targets for Alzheimer’s treatment. In the astrocytes, SREBP cleavage-activating protein (SCAP) binds to Sterol Regulatory Element-binding Protein 2 (SREBP2) in order to transport the complex from the endoplasmic reticulum to the Golgi apparatus. Cholesterol is secreted out of the astrocytes by ATP-Binding Cassette A1 (ABCA1) transporter. Lipoprotein receptors such as triggering receptor expressed on myeloid cells 2 (TREM2) internalize cholesterol into the microglia, while lipoprotein receptors such as Low-density lipoprotein receptor-related protein 1 (LRP1) internalize cholesterol into the neuron. Cytochrome P450 Family 46 Subfamily A Member 1 (CYP46A1) converts excess cholesterol to 24S-hydroxycholesterol (24S-OHC). Cholesterol has been approved for its direct effect on the production of amyloid-beta and tau proteins. The addition of cholesterol to the brain promotes the activity of beta-site amyloid precursor protein cleaving enzyme 1 (BACE1), secretase, and amyloid precursor protein (APP), which all aid in amyloid-beta production. The reduction of cholesterol esters in the brain have been found to reduce phosphorylated tau levels in mice. In this work, a computational pipeline was developed to identify the protein targets involved in cholesterol regulation in brain and further to identify chemical compounds as the inhibitors of a selected protein target. Since extensive evidence shows the strong correlation between brain cholesterol regulation and Alzheimer’s disease, a detailed literature review on genes or pathways related to the brain cholesterol synthesis and regulation was first conducted in this work. An interaction network was then built for those genes so that the top gene targets were identified. The involvement of these genes in Alzheimer’s disease progression was discussed, which was followed by the investigation of existing clinical trials for those targets. A ligand-protein docking program was finally developed to screen 1.5 million chemical compounds for the selected protein target. A machine learning program was developed to evaluate and predict the binding interaction between chemical compounds and the protein target. The results from this work pave the way for further drug discovery to regulate brain cholesterol to combat Alzheimer’s disease. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=Alzheimer%E2%80%99s%20disease" title="Alzheimer’s disease">Alzheimer’s disease</a>, <a href="https://publications.waset.org/abstracts/search?q=drug%20discovery" title=" drug discovery"> drug discovery</a>, <a href="https://publications.waset.org/abstracts/search?q=ligand-protein%20docking" title=" ligand-protein docking"> ligand-protein docking</a>, <a href="https://publications.waset.org/abstracts/search?q=gene-network%20analysis" title=" gene-network analysis"> gene-network analysis</a>, <a href="https://publications.waset.org/abstracts/search?q=cholesterol%20regulation" title=" cholesterol regulation"> cholesterol regulation</a> </p> <a href="https://publications.waset.org/abstracts/162391/a-computational-investigation-of-potential-drugs-for-cholesterol-regulation-to-treat-alzheimers-disease" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/162391.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">75</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">1250</span> Investigations of Protein Aggregation Using Sequence and Structure Based Features</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=M.%20Michael%20Gromiha">M. Michael Gromiha</a>, <a href="https://publications.waset.org/abstracts/search?q=A.%20Mary%20Thangakani"> A. Mary Thangakani</a>, <a href="https://publications.waset.org/abstracts/search?q=Sandeep%20Kumar"> Sandeep Kumar</a>, <a href="https://publications.waset.org/abstracts/search?q=D.%20Velmurugan"> D. Velmurugan</a> </p> <p class="card-text"><strong>Abstract:</strong></p> The main cause of several neurodegenerative diseases such as Alzhemier, Parkinson, and spongiform encephalopathies is formation of amyloid fibrils and plaques in proteins. We have analyzed different sets of proteins and peptides to understand the influence of sequence-based features on protein aggregation process. The comparison of 373 pairs of homologous mesophilic and thermophilic proteins showed that aggregation-prone regions (APRs) are present in both. But, the thermophilic protein monomers show greater ability to ‘stow away’ the APRs in their hydrophobic cores and protect them from solvent exposure. The comparison of amyloid forming and amorphous b-aggregating hexapeptides suggested distinct preferences for specific residues at the six positions as well as all possible combinations of nine residue pairs. The compositions of residues at different positions and residue pairs have been converted into energy potentials and utilized for distinguishing between amyloid forming and amorphous b-aggregating peptides. Our method could correctly identify the amyloid forming peptides at an accuracy of 95-100% in different datasets of peptides. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=aggregation" title="aggregation">aggregation</a>, <a href="https://publications.waset.org/abstracts/search?q=amyloids" title=" amyloids"> amyloids</a>, <a href="https://publications.waset.org/abstracts/search?q=thermophilic%20proteins" title=" thermophilic proteins"> thermophilic proteins</a>, <a href="https://publications.waset.org/abstracts/search?q=amino%20acid%20residues" title=" amino acid residues"> amino acid residues</a>, <a href="https://publications.waset.org/abstracts/search?q=machine%20learning%20techniques" title=" machine learning techniques"> machine learning techniques</a> </p> <a href="https://publications.waset.org/abstracts/20424/investigations-of-protein-aggregation-using-sequence-and-structure-based-features" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/20424.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">614</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">1249</span> Synthesis of Vic-Dioxime Palladium (II) Complex: Precursor for Deposition on SBA-15 in ScCO2</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=As%C4%B1m%20Egitmen">Asım Egitmen</a>, <a href="https://publications.waset.org/abstracts/search?q=Aysen%20Demir"> Aysen Demir</a>, <a href="https://publications.waset.org/abstracts/search?q=Burcu%20Darendeli"> Burcu Darendeli</a>, <a href="https://publications.waset.org/abstracts/search?q=Fatma%20Ulusal"> Fatma Ulusal</a>, <a href="https://publications.waset.org/abstracts/search?q=Bilgehan%20G%C3%BCzel"> Bilgehan Güzel</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Synthesizing supercritical carbon dioxide (scCO<sub>2</sub>) soluble precursors would be helpful for many processes of material syntheses based on scCO<sub>2</sub>. Ligand (a<em>mphi</em>-(1<em>Z</em>, 2Z)-<em>N</em>-(2-fluoro-3-(trifluoromethyl) phenyl)-<em>N</em>'-hydroxy-2-(hydroxyimino) were synthesized from chloro glyoxime and flourus aniline and Pd(II) complex (precursor) prepared. For scCO<sub>2</sub> deposition method, organometallic precursor was dissolved in scCO<sub>2</sub> and impregnated onto the SBA-15 at 90 °C and 3000 psi. Then the organometallic precursor was reduced with H<sub>2</sub> in the CO<sub>2</sub> mixture (150 psi H<sub>2</sub> + 2850 psi CO<sub>2</sub>). Pd deposited support material was characterized by ICP-OES, XRD, FE-SEM, TEM and EDX analyses. The Pd loading of the prepared catalyst, measured by ICP-OES showed a value of about 1.64% mol/g Pd of catalyst. Average particle size was found 5.3 nm. The catalytic activity of prepared catalyst was investigated over Suzuki-Miyaura C-C coupling reaction in different solvent with K<sub>2</sub>CO<sub>3</sub> at 50 <sup>o</sup>C. The conversion ratio was determined by gas chromatography. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=nanoparticle" title="nanoparticle">nanoparticle</a>, <a href="https://publications.waset.org/abstracts/search?q=nanotube" title=" nanotube"> nanotube</a>, <a href="https://publications.waset.org/abstracts/search?q=oximes" title=" oximes"> oximes</a>, <a href="https://publications.waset.org/abstracts/search?q=precursor" title=" precursor"> precursor</a>, <a href="https://publications.waset.org/abstracts/search?q=supercritical%20CO2" title=" supercritical CO2"> supercritical CO2</a> </p> <a href="https://publications.waset.org/abstracts/53003/synthesis-of-vic-dioxime-palladium-ii-complex-precursor-for-deposition-on-sba-15-in-scco2" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/53003.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">356</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">1248</span> Brain Atrophy in Alzheimer's Patients</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Tansa%20Nisan%20Gunerhan">Tansa Nisan Gunerhan</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Dementia comes in different forms, including Alzheimer's disease. The most common dementia diagnosis among elderly individuals is Alzheimer's disease. On average, for patients with Alzheimer’s, life expectancy is around 4-8 years after the diagnosis; however, expectancy can go as high as twenty years or more, depending on the shrinkage of the brain. Normally, along with aging, the brain shrinks at some level but doesn’t lose a vast amount of neurons. However, Alzheimer's patients' neurons are destroyed rapidly; hence problems with loss of memory, communication, and other metabolic activities begin. The toxic changes in the brain affect the stability of the neurons. Beta-amyloid and tau are two proteins that are believed to play a role in the development of Alzheimer's disease through their toxic changes. Beta-amyloid is a protein that is produced in the brain and is normally broken down and removed from the body. However, in people with Alzheimer's disease, the production of beta-amyloid increases, and it begins to accumulate in the brain. These plaques are thought to disrupt communication between nerve cells and may contribute to the death of brain cells. Tau is a protein that helps to stabilize microtubules, which are essential for the transportation of nutrients and other substances within brain cells. In people with Alzheimer's disease, tau becomes abnormal and begins to accumulate inside brain cells, forming neurofibrillary tangles. These tangles disrupt the normal functioning of brain cells and may contribute to their death, forming amyloid plaques which are deposits of a protein called amyloid-beta that build up between nerve cells in the brain. The accumulation of amyloid plaques and neurofibrillary tangles in the brain is thought to contribute to the shrinkage of brain tissue. As the brain shrinks, the size of the brain may decrease, leading to a reduction in brain volume. Brain atrophy in Alzheimer's disease is often accompanied by changes in the structure and function of brain cells and the connections between them, leading to a decline in brain function. These toxic changes that accumulate can cause symptoms such as memory loss, difficulty with thinking and problem-solving, and changes in behavior and personality. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=Alzheimer" title="Alzheimer">Alzheimer</a>, <a href="https://publications.waset.org/abstracts/search?q=amyloid-beta" title=" amyloid-beta"> amyloid-beta</a>, <a href="https://publications.waset.org/abstracts/search?q=brain%20atrophy" title=" brain atrophy"> brain atrophy</a>, <a href="https://publications.waset.org/abstracts/search?q=neuron" title=" neuron"> neuron</a>, <a href="https://publications.waset.org/abstracts/search?q=shrinkage" title=" shrinkage"> shrinkage</a> </p> <a href="https://publications.waset.org/abstracts/161073/brain-atrophy-in-alzheimers-patients" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/161073.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">95</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">1247</span> Towards the Inhibition Mechanism of Lysozyme Fibrillation by Hydrogen Sulfide</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Indra%20Gonzalez%20Ojeda">Indra Gonzalez Ojeda</a>, <a href="https://publications.waset.org/abstracts/search?q=Tatiana%20Quinones"> Tatiana Quinones</a>, <a href="https://publications.waset.org/abstracts/search?q=Manuel%20Rosario"> Manuel Rosario</a>, <a href="https://publications.waset.org/abstracts/search?q=Igor%20Lednev"> Igor Lednev</a>, <a href="https://publications.waset.org/abstracts/search?q=Juan%20Lopez%20Garriga"> Juan Lopez Garriga</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Amyloid fibrils are stable aggregates of misfolded protein associated with many neurodegenerative disorders. It has been shown that hydrogen sulfide (H2S), inhibits the fibrillation of lysozyme through the formation of trisulfide (S-S-S) bonds. However, the overall mechanism remains elusive. Here, the concentration dependence of H2S effect was investigated using Atomic force microscopy (AFM), non-resonance Raman spectroscopy, Deep-UV Raman spectroscopy and circular dichroism (CD). It was found that small spherical aggregates with trisulfide bonds and a unique secondary structure were formed instead of amyloid fibrils when adding concentrations of 25 mM and 50 mM of H2S. This could indicate that H2S might serve as a protecting agent for the protein. However, further characterization of these aggregates and their trisulfide bonds is needed to fully unravel the function H2S has on protein fibrillation. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=amyloid%20fibrils" title="amyloid fibrils">amyloid fibrils</a>, <a href="https://publications.waset.org/abstracts/search?q=hydrogen%20sulfide" title=" hydrogen sulfide"> hydrogen sulfide</a>, <a href="https://publications.waset.org/abstracts/search?q=protein%20folding" title=" protein folding"> protein folding</a>, <a href="https://publications.waset.org/abstracts/search?q=raman%20spectroscopy" title=" raman spectroscopy"> raman spectroscopy</a> </p> <a href="https://publications.waset.org/abstracts/86031/towards-the-inhibition-mechanism-of-lysozyme-fibrillation-by-hydrogen-sulfide" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/86031.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">216</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">1246</span> Functionalized Titanium Dioxide Nanoparticles for Targeting and Disrupting Amyloid Fibrils</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Elad%20Arad">Elad Arad</a>, <a href="https://publications.waset.org/abstracts/search?q=Raz%20Jelinek"> Raz Jelinek</a>, <a href="https://publications.waset.org/abstracts/search?q=Hanna%20Rapaport"> Hanna Rapaport</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Amyloidoses are a family of diseases characterized by abnormal protein folding that leads to aggregation. They accumulate to form fibrillar plaques which are implicated in the pathogenesis of Alzheimer, prion, diabetes type II and other diseases. To the best of our knowledge, despite extensive research efforts devoted to plaque aggregates inhibition, there is yet no cure for this phenomenon. Titanium and its alloys are found in growing interest for biomedical applications. Variety of surface modifications enable porous, adhesive, bioactive coatings for its surface. Titanium oxides (titania) are also being developed for photothermal and photodynamic treatments. Inspired by this, we set to explore the effect of functionalized titania nanoparticles in combination with external stimuli, as potential photothermal ablating agents against amyloids. Titania nanoparticles were coated with bi-functional catechol derivatives (dihydroxy-phenylalanine propanoic acid, noted DPA) to gain targeting properties. In conjunction with UV-radiation, these nanoparticles may selectively destroy the vicinity of their target. Titania modified 5 nm nanoparticles coated with DPA were further conjugated to the amyloid-targeting Congo Red (CR). These Titania-DPA-CR nanoparticles were found to target mature amyloid fibril of both amyloid-β (Aβ 1-42 a.a). Moreover, irradiation of the peptides in presence of the modified nanoparticles decreased the aggregate content and oligomer fraction. This work provides insights into the use of modified titania nanoparticles for amyloid plaque targeting and photothermal destruction. It may shed light on future modifications and functionalization of titania nanoparticles for different applications. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=titanium%20dioxide" title="titanium dioxide">titanium dioxide</a>, <a href="https://publications.waset.org/abstracts/search?q=amyloids" title=" amyloids"> amyloids</a>, <a href="https://publications.waset.org/abstracts/search?q=photothermal%20treatment" title=" photothermal treatment"> photothermal treatment</a>, <a href="https://publications.waset.org/abstracts/search?q=catechol" title=" catechol"> catechol</a>, <a href="https://publications.waset.org/abstracts/search?q=Congo-red" title=" Congo-red"> Congo-red</a> </p> <a href="https://publications.waset.org/abstracts/109975/functionalized-titanium-dioxide-nanoparticles-for-targeting-and-disrupting-amyloid-fibrils" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/109975.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">146</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">1245</span> The Enzyme Inhibitory Potentials of Different Extracts from Linaria genistifolia subsp. genistifolia</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Gokhan%20Zengin">Gokhan Zengin</a>, <a href="https://publications.waset.org/abstracts/search?q=Abdurrahman%20Aktumsek"> Abdurrahman Aktumsek</a> </p> <p class="card-text"><strong>Abstract:</strong></p> The key enzyme inhibitory theory is one of the most accepted strategies in the treatment of global health problems including Alzheimer’s Disease and Diabetes mellitus. For this reason, the enzyme inhibitory potentials of different solvent extracts from Linaria genistifolia subsp. genistifolia were investigated against cholinesterase, and tyrosinase. The in vitro enzyme inhibitory potentials were measured with a microplate reader. The acetone and methanol extracts exhibited the strongest enzyme inhibitory effects on cholinesterase. However, the water extract was only active on tyrosinase. The results suggested that Linaria genistifolia subsp. genistifolia could be considered as a source of natural enzyme inhibitors for the treatment of major health problems. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=enzyme%20inhibitors" title="enzyme inhibitors">enzyme inhibitors</a>, <a href="https://publications.waset.org/abstracts/search?q=cholinesterase" title=" cholinesterase"> cholinesterase</a>, <a href="https://publications.waset.org/abstracts/search?q=tyrosinase" title=" tyrosinase"> tyrosinase</a>, <a href="https://publications.waset.org/abstracts/search?q=linaria" title=" linaria"> linaria</a>, <a href="https://publications.waset.org/abstracts/search?q=Turkey" title=" Turkey"> Turkey</a> </p> <a href="https://publications.waset.org/abstracts/46806/the-enzyme-inhibitory-potentials-of-different-extracts-from-linaria-genistifolia-subsp-genistifolia" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/46806.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">310</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">1244</span> Cytotoxic Effect of Purified and Crude Hyaluronidase Enzyme on Hep G2 Cell Line</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Furqan%20M.%20Kadhum">Furqan M. Kadhum</a>, <a href="https://publications.waset.org/abstracts/search?q=Asmaa%20A.%20Hussein"> Asmaa A. Hussein</a>, <a href="https://publications.waset.org/abstracts/search?q=Maysaa%20Ch.%20Hatem"> Maysaa Ch. Hatem</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Hyaluronidase enzyme was purified from the clinical isolate Staphyloccus aureus in three purification steps, first by precipitation with 90% saturated ammonium sulfate, ion exchange chromatography on DEAE-Cellulose, and gel filtration chromatography throughout Sephacryl S-300. Specific activity of the purified enzyme was reached 930 U/mg protein with 7.4 folds of purification and 46.5% recovery. The enzyme has an average molecular weight of about 69 kDa, with an optimum pH of enzyme activity and stability at pH 7, also the optimum temperature for activity was 37oC. The enzyme was stable with full activity at a temperature ranged between 30-40 oC. Metal ions showed variable inhibitory degree with the strongest effect for Fe+3, however, the chelating and reducing agents had no or little effects. Cytotoxic studies for purified and crude hyaluronidase against cancer cell Hep G2 type at different enzyme concentrations and exposure times showed that the inhibition effect of both crude and purified enzyme increased by increasing the enzyme concentration with no change was observed at 24hr, while at 48 and 72 hrs the same inhibition rate were observed for purified enzyme and differ for the crude filtrate. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=hyaluronidase" title="hyaluronidase">hyaluronidase</a>, <a href="https://publications.waset.org/abstracts/search?q=S.%20aureus" title=" S. aureus"> S. aureus</a>, <a href="https://publications.waset.org/abstracts/search?q=metal%20ions" title=" metal ions"> metal ions</a>, <a href="https://publications.waset.org/abstracts/search?q=cytotoxicity" title=" cytotoxicity"> cytotoxicity</a> </p> <a href="https://publications.waset.org/abstracts/16485/cytotoxic-effect-of-purified-and-crude-hyaluronidase-enzyme-on-hep-g2-cell-line" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/16485.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">447</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">1243</span> Identification of Potential Small Molecule Regulators of PERK Kinase</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Ireneusz%20Majsterek">Ireneusz Majsterek</a>, <a href="https://publications.waset.org/abstracts/search?q=Dariusz%20Pytel"> Dariusz Pytel</a>, <a href="https://publications.waset.org/abstracts/search?q=J.%20Alan%20Diehl"> J. Alan Diehl</a> </p> <p class="card-text"><strong>Abstract:</strong></p> PKR-like ER kinase (PERK) is serine/threonie endoplasmic reticulum (ER) transmembrane kinase activated during ER-stress. PERK can activate signaling pathways known as unfolded protein response (UPR). Attenuation of translation is mediated by PERK via phosphorylation of eukaryotic initiation factor 2α (eIF2α), which is necessary for translation initiation. PERK activation also directly contributes to activation of Nrf2 which regulates expression of anti-oxidant enzymes. An increased phosphorylation of eIF2α has been reported in Alzheimer disease (AD) patient hippocampus, indicating that PERK is activated in this disease. Recent data have revealed activation of PERK signaling in non-Hodgkins lymphomas. Results also revealed that loss of PERK limits mammary tumor cell growth in vitro and in vivo. Consistent with these observations, activation of UPR in vitro increases levels of the amyloid precursor protein (APP), the peptide from which beta-amyloid plaques (AB) fragments are derived. Finally, proteolytic processing of APP, including the cleavages that produce AB, largely occurs in the ER, and localization coincident with PERK activity. Thus, we expect that PERK-dependent signaling is critical for progression of many types of diseases (human cancer, neurodegenerative disease and other). Therefore, modulation of PERK activity may be a useful therapeutic target in the treatment of different diseases that fail to respond to traditional chemotherapeutic strategies, including Alzheimer’s disease. Our goal will be to developed therapeutic modalities targeting PERK activity. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=PERK%20kinase" title="PERK kinase">PERK kinase</a>, <a href="https://publications.waset.org/abstracts/search?q=small%20molecule%20inhibitor" title=" small molecule inhibitor"> small molecule inhibitor</a>, <a href="https://publications.waset.org/abstracts/search?q=neurodegenerative%20disease" title=" neurodegenerative disease"> neurodegenerative disease</a>, <a href="https://publications.waset.org/abstracts/search?q=Alzheimer%E2%80%99s%20disease" title=" Alzheimer’s disease"> Alzheimer’s disease</a> </p> <a href="https://publications.waset.org/abstracts/18276/identification-of-potential-small-molecule-regulators-of-perk-kinase" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/18276.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">482</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">1242</span> Role of GM1 in the Interaction between Amyloid Prefibrillar Oligomers of Salmon Calcitonin and Model Membranes</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Cristiano%20Giordani">Cristiano Giordani</a>, <a href="https://publications.waset.org/abstracts/search?q=Marco%20Diociaiuti"> Marco Diociaiuti</a>, <a href="https://publications.waset.org/abstracts/search?q=Cecilia%20Bombelli"> Cecilia Bombelli</a>, <a href="https://publications.waset.org/abstracts/search?q=Laura%20Zanetti-Polzi"> Laura Zanetti-Polzi</a>, <a href="https://publications.waset.org/abstracts/search?q=Marcello%20Belfiore"> Marcello Belfiore</a>, <a href="https://publications.waset.org/abstracts/search?q=Raoul%20Fioravanti"> Raoul Fioravanti</a>, <a href="https://publications.waset.org/abstracts/search?q=Gianfranco%20Macchia"> Gianfranco Macchia</a> </p> <p class="card-text"><strong>Abstract:</strong></p> We investigated induced functional effects by evaluating Ca2+-influx in liposomes and cell viability in HT22-DIFF neurons. Only solutions rich in unstructured Prefibrillar-Oligomers (PFOs) were able, in the presence of Monosialoganglioside-GM1 (GM1), to induce Ca2+-influx and were also neurotoxic, suggesting a correlation between the two phenomena. Thus, in the presence of GM1, we investigated the protein conformation and liposome modification due to the interaction. Circular Dichroism showed that GM1 fostered the formation of β-structures and Energy Filtered-Transmission Electron Microscopy that PFOs formed “amyloid-channels” as reported for Aβ. We speculate that electrostatic forces occurring between the positive PFOs and negative GM1 drive the initial binding, while the hydrophobic profile of the flexible PFO is responsible for the subsequent pore formation. Conversely, the rigid β-structured mature/fibers (MFs) and proto-fibers (PFs) were unable to induce membrane damage and Ca2+- influx. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=amyloid%20proteins" title="amyloid proteins">amyloid proteins</a>, <a href="https://publications.waset.org/abstracts/search?q=neurotoxicity" title=" neurotoxicity"> neurotoxicity</a>, <a href="https://publications.waset.org/abstracts/search?q=lipid-rafts" title=" lipid-rafts"> lipid-rafts</a>, <a href="https://publications.waset.org/abstracts/search?q=GM1" title=" GM1"> GM1</a> </p> <a href="https://publications.waset.org/abstracts/118119/role-of-gm1-in-the-interaction-between-amyloid-prefibrillar-oligomers-of-salmon-calcitonin-and-model-membranes" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/118119.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">189</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">1241</span> Tripeptide Inhibitor: The Simplest Aminogenic PEGylated Drug against Amyloid Beta Peptide Fibrillation</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Sutapa%20Som%20Chaudhury">Sutapa Som Chaudhury</a>, <a href="https://publications.waset.org/abstracts/search?q=Chitrangada%20Das%20Mukhopadhyay"> Chitrangada Das Mukhopadhyay</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Alzheimer’s disease is a well-known form of dementia since its discovery in 1906. Current Food and Drug Administration approved medications e.g. cholinesterase inhibitors, memantine offer modest symptomatic relief but do not play any role in disease modification or recovery. In last three decades many small molecules, chaperons, synthetic peptides, partial β-secretase enzyme blocker have been tested for the development of a drug against Alzheimer though did not pass the 3rd clinical phase trials. Here in this study, we designed a PEGylated, aminogenic, tripeptidic polymer with two different molecular weights based on the aggregation prone amino acid sequence 17-20 in amyloid beta (Aβ) 1-42. Being conjugated with poly-ethylene glycol (PEG) which self-assembles into hydrophilic nanoparticles, these PEGylated tripeptides constitute a very good drug delivery system crossing the blood brain barrier while the peptide remains protected from proteolytic degradation and non-specific protein interactions. Moreover, being completely aminogenic they would not raise any side effects. These peptide inhibitors were evaluated for their effectiveness against Aβ42 fibrillation at an early stage of oligomer to fibril formation as well as preformed fibril clearance via Thioflavin T (ThT) assay, dynamic light scattering analyses, atomic force microscopy and scanning electron microscopy. The inhibitors were proved to be safe at a higher concentration of 20µM by the reduction assay of 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT) dye. Moreover, SHSY5Y neuroblastoma cells have shown a greater survivability when treated with the inhibitors following Aβ42 fibril and oligomer treatment as compared with the control Aβ42 fibril and/or oligomer treated neuroblastoma cells. These make the peptidic inhibitors a promising compound in the aspect of the discovery of alternative medication for Alzheimer’s disease. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=Alzheimer%E2%80%99s%20disease" title="Alzheimer’s disease">Alzheimer’s disease</a>, <a href="https://publications.waset.org/abstracts/search?q=alternative%20medication" title=" alternative medication"> alternative medication</a>, <a href="https://publications.waset.org/abstracts/search?q=amyloid%20beta" title=" amyloid beta"> amyloid beta</a>, <a href="https://publications.waset.org/abstracts/search?q=PEGylated%20peptide" title=" PEGylated peptide"> PEGylated peptide</a> </p> <a href="https://publications.waset.org/abstracts/74111/tripeptide-inhibitor-the-simplest-aminogenic-pegylated-drug-against-amyloid-beta-peptide-fibrillation" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/74111.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">209</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">1240</span> Production of Linamarase from Lactobacillus delbrueckii NRRL B-763</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Ogbonnaya%20Nwokoro">Ogbonnaya Nwokoro</a>, <a href="https://publications.waset.org/abstracts/search?q=Florence%20O.%20Anya"> Florence O. Anya</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Nutritional factors relating to the production of linamarase from Lactobacillus delbrueckii NRRL B–763 were investigated. The microorganism was cultivated in a medium containing 1% linamarin. Enzyme was produced using a variety of carbon substrates but the highest enzyme activity was detected in the presence of salicin (522 U/ml) after 48 h while the lowest yield was observed with CM cellulose (38 U/ml) after 72 h. Enzyme was not produced in the presence of cellobiose. Among a variety of nitrogen substrates tested, peptone supported maximum enzyme production (412 U/ml) after 48 h. Lowest enzyme production was observed with urea (40 U/ml). Organic nitrogen substrates generally supported higher enzyme productivity than inorganic nitrogen substrates. Enzyme activity was observed in the presence of Mn2+ (% relative activity = 216) while Hg2+ was inhibitory (% relative activity = 28). Locally-formulated media were comparable to MRS broth in supporting linamarase production by the bacterium. Higher enzyme activity was produced in media with surfactant than in media without surfactant. The enzyme may be useful in enhanced degradation of cassava cyanide. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=linamarase" title="linamarase">linamarase</a>, <a href="https://publications.waset.org/abstracts/search?q=locally%20formulated%20media" title=" locally formulated media"> locally formulated media</a>, <a href="https://publications.waset.org/abstracts/search?q=carbon%20substrates" title=" carbon substrates"> carbon substrates</a>, <a href="https://publications.waset.org/abstracts/search?q=nitrogen%20substrates" title=" nitrogen substrates"> nitrogen substrates</a>, <a href="https://publications.waset.org/abstracts/search?q=metal%20ions" title=" metal ions "> metal ions </a> </p> <a href="https://publications.waset.org/abstracts/14419/production-of-linamarase-from-lactobacillus-delbrueckii-nrrl-b-763" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/14419.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">427</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">1239</span> Effect of Ethanol Concentration and Enzyme Pre-Treatment on Bioactive Compounds from Ginger Extract</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=S.%20Lekhavat">S. Lekhavat</a>, <a href="https://publications.waset.org/abstracts/search?q=T.%20Kajsongkram"> T. Kajsongkram</a>, <a href="https://publications.waset.org/abstracts/search?q=S.%20Sang-han"> S. Sang-han</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Dried ginger was extracted and investigated the effect of ethanol concentration and enzyme pre-treatment on its bioactive compounds in solvent extraction process. Sliced fresh gingers were dried by oven dryer at 70 °C for 24 hours and ground to powder using grinder which their size were controlled by passing through a 20-mesh sieve. In enzyme pre-treatment process, ginger powder was sprayed with 1 % (w/w) cellulase and then was incubated at 45 °C for 2 hours following by extraction process using ethanol at concentration of 0, 20, 40, 60 and 80 % (v/v), respectively. The ratio of ginger powder and ethanol are 1:9 and extracting conditions were controlled at 80 °C for 2 hours. Bioactive compounds extracted from ginger, either enzyme-treated or non enzyme-treated samples, such as total phenolic content (TPC), 6-Gingerol (6 G), 6-Shogaols (6 S) and antioxidant activity (IC50 using DPPH assay), were examined. Regardless of enzyme treatment, the results showed that 60 % ethanol provided the highest TPC (20.36 GAE mg /g. dried ginger), 6G (0.77%), 6S (0.036 %) and the lowest IC50 (625 μg/ml) compared to other ratios of ethanol. Considering the effect of enzyme on bioactive compounds and antioxidant activity, it was found that enzyme-treated sample has more 6G (0.17-0.77 %) and 6S (0.020-0.036 %) than non enzyme-treated samples (0.13-0.77 % 6G, 0.015-0.036 % 6S). However, the results showed that non enzyme-treated extracts provided higher TPC (6.76-20.36 GAE mg /g. dried ginger) and Lowest IC50 (625-1494 μg/ml ) than enzyme-treated extracts (TPC 5.36-17.50 GAE mg /g. dried ginger, IC50 793-2146 μg/ml). <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=antioxidant%20activity" title="antioxidant activity">antioxidant activity</a>, <a href="https://publications.waset.org/abstracts/search?q=enzyme" title=" enzyme"> enzyme</a>, <a href="https://publications.waset.org/abstracts/search?q=extraction" title=" extraction"> extraction</a>, <a href="https://publications.waset.org/abstracts/search?q=ginger" title=" ginger"> ginger</a> </p> <a href="https://publications.waset.org/abstracts/53148/effect-of-ethanol-concentration-and-enzyme-pre-treatment-on-bioactive-compounds-from-ginger-extract" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/53148.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">256</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">1238</span> Synthesis and Characterization of CaZrTi2O7 from Tartrate Precursor Employing Microwave Heating Technique</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=B.%20M.%20Patil">B. M. Patil</a>, <a href="https://publications.waset.org/abstracts/search?q=S.%20R.%20Dharwadkar"> S. R. Dharwadkar</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Zirconolite (CaZrTi2O7) is one of the three major phases in the synthetic ceramic 'SYNROC' which is used for immobilization of high-level nuclear waste and also acts as photocatalytic and photophysical properties. In the present work the nanocrystalline CaZrTi2O7 was synthesized from Calcium Zirconyl Titanate tartrate precursor (CZTT) employing two different heating techniques such as Conventional heating (Muffle furnace) and Microwave heating (Microwave Oven). Thermal decomposition of the CZTT precursors in air yielded nanocrystalline CaZrTi2O7 powder as the end product. The products obtained by annealing the CZTT precursor using both heating method were characterized using simultaneous TG-DTA, FTIR, XRD, SEM, TEM, NTA and thermodilatometric study. The physical characteristics such as crystallinity, morphology and particle size of the product obtained by heating the CZTT precursor at the different temperatures in a Muffle furnace and Microwave oven were found to be significantly different. The microwave heating technique considerably lowered the synthesis temperature of CaZrTi2O7. The influence of microwave heating was more pronounced as compared to Muffle furnace heating. The details of the synthesis of CaZrTi2O7 from CZTT precursor are discussed. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=CZTT" title="CZTT">CZTT</a>, <a href="https://publications.waset.org/abstracts/search?q=CaZrTi2O7" title=" CaZrTi2O7"> CaZrTi2O7</a>, <a href="https://publications.waset.org/abstracts/search?q=microwave" title=" microwave"> microwave</a>, <a href="https://publications.waset.org/abstracts/search?q=SYNROC" title=" SYNROC"> SYNROC</a>, <a href="https://publications.waset.org/abstracts/search?q=zirconolite" title=" zirconolite "> zirconolite </a> </p> <a href="https://publications.waset.org/abstracts/79296/synthesis-and-characterization-of-cazrti2o7-from-tartrate-precursor-employing-microwave-heating-technique" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/79296.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">165</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">1237</span> Optical Characterization and Surface Morphology of SnO2 Thin Films Prepared by Spin Coating Technique</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=J.%20O.%20Ajayi">J. O. Ajayi</a>, <a href="https://publications.waset.org/abstracts/search?q=S.%20S.%20Oluyamo"> S. S. Oluyamo</a>, <a href="https://publications.waset.org/abstracts/search?q=D.%20B.%20Agunbiade"> D. B. Agunbiade</a> </p> <p class="card-text"><strong>Abstract:</strong></p> In this work, tin oxide thin films (SnO2) were prepared using the spin coating technique. The effects of precursor concentration on the thin film properties were investigated. Tin oxide was synthesized from anhydrous Tin (II) Chloride (SnCl2) dispersed in Methanol and Acetic acid. The metallic oxide (SnO2) films deposited were characterized using the UV Spectrophotometer and the Scanning Electron Microscope (SEM). From the absorption spectra, absorption increases with decrease in precursor concentration. Absorbance in the VIS region is lower than 0 % at higher concentration. The optical transmission spectrum shows that transmission increases as the concentration of precursor decreases and the maximum transmission in visible region is about 90% for films prepared with 0.2 M. Also, there is increase in the reflectance of thin films as concentration of precursor increases. The films have high transparency (more than 85%) and low reflectance (less than 40%) in the VIS region. Investigation showed that the direct band gap value increased from 3.79eV, to 3.82eV as the precursor concentration decreased from 0.6 M to 0.2 M. Average direct bandgap energy for all the tin oxide films was estimated to be 3.80eV. The effect of precursor concentration was directly observed in crystal outgrowth and surface particle densification. They were found to increase proportionately with higher concentration. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=anhydrous%20TIN%20%28II%29%20chloride" title="anhydrous TIN (II) chloride">anhydrous TIN (II) chloride</a>, <a href="https://publications.waset.org/abstracts/search?q=densification" title=" densification"> densification</a>, <a href="https://publications.waset.org/abstracts/search?q=NIS-%20VIS%20region" title=" NIS- VIS region"> NIS- VIS region</a>, <a href="https://publications.waset.org/abstracts/search?q=spin%20coating%20technique" title=" spin coating technique"> spin coating technique</a> </p> <a href="https://publications.waset.org/abstracts/31411/optical-characterization-and-surface-morphology-of-sno2-thin-films-prepared-by-spin-coating-technique" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/31411.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">261</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">1236</span> The Interaction between Blood-Brain Barrier and the Cerebral Lymphatics Proposes Therapeutic Method for Alzheimer’S Disease </h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=M.%20Klimova">M. Klimova</a>, <a href="https://publications.waset.org/abstracts/search?q=O.%20Semyachkina-Glushkovskaya"> O. Semyachkina-Glushkovskaya</a>, <a href="https://publications.waset.org/abstracts/search?q=J.%20Kurts"> J. Kurts</a>, <a href="https://publications.waset.org/abstracts/search?q=E.%20Zinchenko"> E. Zinchenko</a>, <a href="https://publications.waset.org/abstracts/search?q=N.%20Navolokin"> N. Navolokin</a>, <a href="https://publications.waset.org/abstracts/search?q=A.%20Shirokov"> A. Shirokov</a>, <a href="https://publications.waset.org/abstracts/search?q=A.%20Dubrovsky"> A. Dubrovsky</a>, <a href="https://publications.waset.org/abstracts/search?q=A.%20Abdurashitov"> A. Abdurashitov</a>, <a href="https://publications.waset.org/abstracts/search?q=A.%20Terskov"> A. Terskov</a>, <a href="https://publications.waset.org/abstracts/search?q=A.%20Mamedova"> A. Mamedova</a>, <a href="https://publications.waset.org/abstracts/search?q=I.%20Agranovich"> I. Agranovich</a>, <a href="https://publications.waset.org/abstracts/search?q=T.%20Antonova"> T. Antonova</a>, <a href="https://publications.waset.org/abstracts/search?q=I.%20Blokhina"> I. Blokhina</a> </p> <p class="card-text"><strong>Abstract:</strong></p> The direction for research of Alzheimer's disease is to find an effective non-invasive and non-pharmacological way of treatment. Here we tested our hypothesis that the opening of the blood-brain barrier (BBB) induces activation of lymphatic drainage and clearing functions that can be used as a method for non-invasive stimulation of clearance of beta-amyloid and therapy of Alzheimer’s disease (AD). To test our hypothesis, in this study on healthy male mice we analyzed the interaction between BBB opening by repeated loud music (100-10000 Hz, 100 dB, duration 2 h: 60 sec – sound; 60 sec - pause) and functional changes in the meningeal lymphatic vessels (MLVs). We demonstrate clearance of dextran 70 kDa (i.v. injection), fluorescent beta-amyloid (intrahippocampal injection) and gold nanorods (intracortical injection) via MLV that significantly increased after the opening of BBB. Our studies also demonstrate that the BBB opening was associated with the improvement of neurocognitive status in mice with AD. Thus, we uncover therapeutic effects of BBB opening by loud music, such as non-invasive stimulation of lymphatic clearance of beta-amyloid in mice with AD, accompanied by improvement of their neurocognitive status. Our data are consistent with other results suggesting the therapeutic effect of BBB opening by focused ultrasound without drugs for patients with AD. This research was supported by a grant from RSF 18-75-10033 <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=Alzheimer%27s%20disease" title="Alzheimer's disease">Alzheimer's disease</a>, <a href="https://publications.waset.org/abstracts/search?q=beta-amyloid" title=" beta-amyloid"> beta-amyloid</a>, <a href="https://publications.waset.org/abstracts/search?q=blood-brain%20barrier" title=" blood-brain barrier"> blood-brain barrier</a>, <a href="https://publications.waset.org/abstracts/search?q=meningeal%20lymphatic%20vessels" title=" meningeal lymphatic vessels"> meningeal lymphatic vessels</a>, <a href="https://publications.waset.org/abstracts/search?q=repeated%20loud%20music" title=" repeated loud music"> repeated loud music</a> </p> <a href="https://publications.waset.org/abstracts/122385/the-interaction-between-blood-brain-barrier-and-the-cerebral-lymphatics-proposes-therapeutic-method-for-alzheimers-disease" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/122385.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">142</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">1235</span> The Modeling of Viscous Microenvironment for the Coupled Enzyme System of Bioluminescence Bacteria </h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Irina%20E.%20Sukovataya">Irina E. Sukovataya</a>, <a href="https://publications.waset.org/abstracts/search?q=Oleg%20S.%20Sutormin"> Oleg S. Sutormin</a>, <a href="https://publications.waset.org/abstracts/search?q=Valentina%20A.%20Kratasyuk"> Valentina A. Kratasyuk </a> </p> <p class="card-text"><strong>Abstract:</strong></p> Effect of viscosity of media on kinetic parameters of the coupled enzyme system NADH:FMN-oxidoreductase–luciferase was investigated with addition of organic solvents (glycerol and sucrose), because bioluminescent enzyme systems based on bacterial luciferases offer a unique and general tool for analysis of the many analytes and enzymes in the environment, research, and clinical laboratories and other fields. The possibility of stabilization and increase of activity of the coupled enzyme system NADH:FMN-oxidoreductase–luciferase activity in vicious aqueous-organic mixtures have been shown. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=coupled%20enzyme%20system%20of%20bioluminescence%20bacteria%20NAD%28P%29H%3AFMN-oxidoreductase%E2%80%93luciferase" title="coupled enzyme system of bioluminescence bacteria NAD(P)H:FMN-oxidoreductase–luciferase">coupled enzyme system of bioluminescence bacteria NAD(P)H:FMN-oxidoreductase–luciferase</a>, <a href="https://publications.waset.org/abstracts/search?q=glycerol" title=" glycerol"> glycerol</a>, <a href="https://publications.waset.org/abstracts/search?q=stabilization%20of%20enzymes" title=" stabilization of enzymes"> stabilization of enzymes</a>, <a href="https://publications.waset.org/abstracts/search?q=sucrose" title=" sucrose"> sucrose</a> </p> <a href="https://publications.waset.org/abstracts/2372/the-modeling-of-viscous-microenvironment-for-the-coupled-enzyme-system-of-bioluminescence-bacteria" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/2372.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">395</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">1234</span> Mapping Protein Selectivity Landscapes</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Niv%20Papo">Niv Papo</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Characterizing the binding selectivity landscape of interacting proteins is crucial both for elucidating the underlying mechanisms of their interaction and for developing selective inhibitors. However, current mapping methods are laborious and cannot provide a sufficiently comprehensive description of the landscape. Here, we introduce a distinct and efficient strategy for comprehensively mapping the binding landscape of proteins using a combination of experimental multi-target selective library screening and in silico next-generation sequencing analysis. We map the binding landscape of a non-selective trypsin inhibitor, the amyloid protein precursor inhibitor (APPI), to each of four human serine proteases (kallikrein-6, mesotrypsin, and anionic and cationic trypsins). We then use this map to dissect and improve the affinity and selectivity of APPI variants toward each of the four proteases. Our strategy can be used as a platform for the development of a new generation of target-selective probes and therapeutic agents based on selective protein–protein interactions. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=drug%20design" title="drug design">drug design</a>, <a href="https://publications.waset.org/abstracts/search?q=directed%20evolution" title=" directed evolution"> directed evolution</a>, <a href="https://publications.waset.org/abstracts/search?q=protein%20engineering" title=" protein engineering"> protein engineering</a>, <a href="https://publications.waset.org/abstracts/search?q=protease%20inhibition." title=" protease inhibition."> protease inhibition.</a> </p> <a href="https://publications.waset.org/abstracts/191315/mapping-protein-selectivity-landscapes" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/191315.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">24</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">1233</span> Quality of Low Fat Traditional Pork Sausage Containing Transglutaminase</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Jiraporn%20Burakorn">Jiraporn Burakorn</a>, <a href="https://publications.waset.org/abstracts/search?q=Pran%20Pinthong"> Pran Pinthong</a>, <a href="https://publications.waset.org/abstracts/search?q=Supida%20Hutabaedya"> Supida Hutabaedya</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Commercial traditional pork sausages (Moo Yaw) were produced by added more than 30% of pork fat for appetite customer. The pork sausages texture were softness, firmness, juiciness and smooth. If the pork sausages contained less fat, their textures were hardness, dryness and incoherence. This research investigated production of low fat traditional pork sausage containing transglutaminase for improved its sensory properties and nutritive values. The enzyme pork sausage composed of transglutaminase, soybean cake, rice bran oil and other ingredients. Consumer acceptance test was done by comparing the enzyme pork sausage with the 3 commercial pork sausage with 95 consumer. The enzyme pork sausage was accepted 92.6% and was preferred in all attributes over the 3 commercial pork sausages such as appearance, color, flavor, taste, firmness and overall liking. The enzyme pork sausage was high protein but low total calories, calories from fat, total fat, saturated fat, cholesterol and carbohydrate. The enzyme pork sausage was lower calorie (90 kcal) than the commercial reference pork sausage (150 kcal) 64%. The morphological texture of the enzyme pork sausage was smooth and consistency when analyzed by SEM. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=low%20fat" title="low fat">low fat</a>, <a href="https://publications.waset.org/abstracts/search?q=Moo%20Yaw" title=" Moo Yaw"> Moo Yaw</a>, <a href="https://publications.waset.org/abstracts/search?q=pork%20sausage" title=" pork sausage"> pork sausage</a>, <a href="https://publications.waset.org/abstracts/search?q=transglutaminase" title=" transglutaminase"> transglutaminase</a> </p> <a href="https://publications.waset.org/abstracts/58317/quality-of-low-fat-traditional-pork-sausage-containing-transglutaminase" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/58317.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">230</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">1232</span> Enzyme Immobilization on Functionalized Polystyrene Nanofibersfor Bioprocessing Applications</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Mailin%20Misson">Mailin Misson</a>, <a href="https://publications.waset.org/abstracts/search?q=Bo%20Jin"> Bo Jin</a>, <a href="https://publications.waset.org/abstracts/search?q=Sheng%20Dai"> Sheng Dai</a>, <a href="https://publications.waset.org/abstracts/search?q=Hu%20Zhang"> Hu Zhang</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Advances in biotechnology have witnessed a growing interest in enzyme applications for the development of green and sustainable bio processes. While known as powerful bio catalysts, enzymes are no longer of economic value when extended to large commercialization. Alternatively, immobilization technology allows enzyme recovery and continuous reuse which subsequently compensates high operating costs. Employment of enzymes on nano structured materials has been recognized as a promising approach to enhance enzyme catalytic performances. High porosity, inter connectivity and self-assembling behaviors endow nano fibers as exciting candidate for enzyme carrier in bio reactor systems. In this study, nano fibers were successfully fabricated via electro spinning system by optimizing the polymer concentration (10-30 %, w/v), applied voltage (10-30 kV) and discharge distance (11-26 cm). Microscopic images have confirmed the quality as homogeneous and good fiber alignment. The nano fibers surface was modified using strong oxidizing agent to facilitate bio molecule binding. Bovine serum albumin and β-galactosidase enzyme were employed as model bio catalysts and immobilized onto the oxidized surfaces through covalent binding. Maximum enzyme adsorption capacity of the modified nano fibers was 3000 mg/g, 3-fold higher than the unmodified counterpart (1000 mg/g). The highest immobilization yield was 80% and reached the saturation point at 2 mg/ml of enzyme concentration. The results indicate a significant increase of activity retention by the enzyme-bound modified nano fibers (80%) as compared to the nascent one (60%), signifying excellent enzyme-nano carrier bio compatibility. The immobilized enzyme was further used for the bio conversion of dairy wastes into value-added products. This study demonstrates great potential of acid-modified electrospun polystyrene nano fibers as enzyme carriers. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=immobilization" title="immobilization">immobilization</a>, <a href="https://publications.waset.org/abstracts/search?q=enzyme" title=" enzyme"> enzyme</a>, <a href="https://publications.waset.org/abstracts/search?q=nanocarrier" title=" nanocarrier"> nanocarrier</a>, <a href="https://publications.waset.org/abstracts/search?q=nanofibers" title=" nanofibers"> nanofibers</a> </p> <a href="https://publications.waset.org/abstracts/15802/enzyme-immobilization-on-functionalized-polystyrene-nanofibersfor-bioprocessing-applications" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/15802.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">293</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">1231</span> CuO Thin Films Deposition by Spray Pyrolysis: Influence of Precursor Solution Properties</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=M.%20Lamri%20Zeggar">M. Lamri Zeggar</a>, <a href="https://publications.waset.org/abstracts/search?q=F.%20Bourfaa"> F. Bourfaa</a>, <a href="https://publications.waset.org/abstracts/search?q=A.%20Adjimi"> A. Adjimi</a>, <a href="https://publications.waset.org/abstracts/search?q=F.%20Boutebakh"> F. Boutebakh</a>, <a href="https://publications.waset.org/abstracts/search?q=M.%20S.%20Aida"> M. S. Aida</a>, <a href="https://publications.waset.org/abstracts/search?q=N.%20Attaf"> N. Attaf</a> </p> <p class="card-text"><strong>Abstract:</strong></p> CuO thin films were deposited by spray ultrasonic pyrolysis with different precursor solution. Two staring solution slats were used namely: Copper acetate and copper chloride. The influence of these solutions on CuO thin films proprieties of is instigated. The X rays diffraction (XDR) analysis indicated that the films deposed with copper acetate are amorphous however the films elaborated with copper chloride have monoclinic structure. UV- Visible transmission spectra showed a strong absorbance of the deposited CuO thin films in the visible region. Electrical characterization has shown that CuO thin films prepared with copper acetate have a higher electrical conductivity. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=thin%20films" title="thin films">thin films</a>, <a href="https://publications.waset.org/abstracts/search?q=cuprous%20oxide" title=" cuprous oxide"> cuprous oxide</a>, <a href="https://publications.waset.org/abstracts/search?q=spray%20pyrolysis" title=" spray pyrolysis"> spray pyrolysis</a>, <a href="https://publications.waset.org/abstracts/search?q=precursor%20solution" title=" precursor solution"> precursor solution</a> </p> <a href="https://publications.waset.org/abstracts/36338/cuo-thin-films-deposition-by-spray-pyrolysis-influence-of-precursor-solution-properties" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/36338.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">311</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">1230</span> Text Mining Techniques for Prioritizing Pathogenic Mutations in Protein Families Known to Misfold or Aggregate</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Khaleel%20Saleh%20Al-Rababah">Khaleel Saleh Al-Rababah</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Amyloid fibril forming regions, which are known as protein aggregates, in sequences of some protein families are associated with a number of diseases known as amyloidosis. Mutations play a role in forming fibrils by accelerating the fibril formation process. In this paper we want to extract diseases that caused by those mutations as a result of the impact of the mutations on structural and functional properties of the aggregated protein. We propose a text mining system, to automatically extract mutations, diseases and relations between mutations and diseases. We presented an algorithm based on finite state to cluster mutations found in the same sentence as a sentence could contain different mutation cause different diseases. Also, we presented a co reference algorithm that enables cross-link sentences. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=amyloid" title="amyloid">amyloid</a>, <a href="https://publications.waset.org/abstracts/search?q=amyloidosis" title=" amyloidosis"> amyloidosis</a>, <a href="https://publications.waset.org/abstracts/search?q=co%20reference" title=" co reference"> co reference</a>, <a href="https://publications.waset.org/abstracts/search?q=protein" title=" protein"> protein</a>, <a href="https://publications.waset.org/abstracts/search?q=text%20mining" title=" text mining"> text mining</a> </p> <a href="https://publications.waset.org/abstracts/24232/text-mining-techniques-for-prioritizing-pathogenic-mutations-in-protein-families-known-to-misfold-or-aggregate" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/24232.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">526</span> </span> </div> </div> <ul class="pagination"> <li class="page-item disabled"><span class="page-link">&lsaquo;</span></li> <li class="page-item active"><span class="page-link">1</span></li> <li class="page-item"><a class="page-link" href="https://publications.waset.org/abstracts/search?q=%CE%B2-site%20amyloid%20precursor%20protein-cleaving%20enzyme%201&page=2">2</a></li> <li class="page-item"><a class="page-link" href="https://publications.waset.org/abstracts/search?q=%CE%B2-site%20amyloid%20precursor%20protein-cleaving%20enzyme%201&page=3">3</a></li> <li class="page-item"><a class="page-link" href="https://publications.waset.org/abstracts/search?q=%CE%B2-site%20amyloid%20precursor%20protein-cleaving%20enzyme%201&page=4">4</a></li> <li class="page-item"><a class="page-link" href="https://publications.waset.org/abstracts/search?q=%CE%B2-site%20amyloid%20precursor%20protein-cleaving%20enzyme%201&page=5">5</a></li> <li class="page-item"><a class="page-link" href="https://publications.waset.org/abstracts/search?q=%CE%B2-site%20amyloid%20precursor%20protein-cleaving%20enzyme%201&page=6">6</a></li> <li class="page-item"><a class="page-link" href="https://publications.waset.org/abstracts/search?q=%CE%B2-site%20amyloid%20precursor%20protein-cleaving%20enzyme%201&page=7">7</a></li> <li class="page-item"><a class="page-link" href="https://publications.waset.org/abstracts/search?q=%CE%B2-site%20amyloid%20precursor%20protein-cleaving%20enzyme%201&page=8">8</a></li> <li class="page-item"><a class="page-link" href="https://publications.waset.org/abstracts/search?q=%CE%B2-site%20amyloid%20precursor%20protein-cleaving%20enzyme%201&page=9">9</a></li> <li class="page-item"><a class="page-link" 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