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inhibition.</title> <meta name="description" content="Search results for: protease inhibition."> <meta name="keywords" content="protease inhibition."> <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 Excellence" title="Open Science Research Excellence" /> </a> <button class="d-block d-lg-none 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action="https://publications.waset.org/abstracts/search"> <div id="custom-search-input"> <div class="input-group"> <i class="fas fa-search"></i> <input type="text" class="search-query" name="q" placeholder="Author, Title, Abstract, Keywords" value="protease inhibition."> <input type="submit" class="btn_search" value="Search"> </div> </div> </form> </div> </div> <div class="row mt-3"> <div class="col-sm-3"> <div class="card"> <div class="card-body"><strong>Commenced</strong> in January 2007</div> </div> </div> <div class="col-sm-3"> <div class="card"> <div class="card-body"><strong>Frequency:</strong> Monthly</div> </div> </div> <div class="col-sm-3"> <div class="card"> <div class="card-body"><strong>Edition:</strong> International</div> </div> </div> <div class="col-sm-3"> <div class="card"> <div class="card-body"><strong>Paper Count:</strong> 1097</div> </div> </div> </div> <h1 class="mt-3 mb-3 text-center" style="font-size:1.6rem;">Search results for: protease inhibition.</h1> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">1097</span> Isolation of Protease Producing Bacteria from Soil Sediments of Ayiramthengu Mangrove Ecosystem</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Reshmi%20Vijayan">Reshmi Vijayan</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Alkaline protease is one of the most important enzymes in the biological world. Microbial production of alkaline protease is getting more attention from researchers due to its unique properties and substantial activity. Microorganisms are the most common sources of commercial enzymes due to their physiological and biochemical properties. The study was conducted on Ayiramthenghu mangrove sediments to isolate protease producing bacteria. All the isolates were screened for proteolytic activity on a skim milk agar plate at 37˚C for 48hrs. Protease activities were determined by the formation of a clear zone around the colonies on Skim milk agar medium. The activity of the enzyme was measured by the tyrosine standard curve, and it was found to be 0.186285 U/ml/min. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=protease" title="protease">protease</a>, <a href="https://publications.waset.org/abstracts/search?q=protease%20assay" title=" protease assay"> protease assay</a>, <a href="https://publications.waset.org/abstracts/search?q=skim%20milk%20agar%20medium" title=" skim milk agar medium"> skim milk agar medium</a>, <a href="https://publications.waset.org/abstracts/search?q=mangrove%20ecosystem" title=" mangrove ecosystem"> mangrove ecosystem</a> </p> <a href="https://publications.waset.org/abstracts/168883/isolation-of-protease-producing-bacteria-from-soil-sediments-of-ayiramthengu-mangrove-ecosystem" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/168883.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">98</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">1096</span> A Promising Thrombolytic and Anticoagulant Serine Protease Purified from Lug Worms Inhabiting Tidal Flats</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Hye%20Jin%20Kim">Hye Jin Kim</a>, <a href="https://publications.waset.org/abstracts/search?q=Hwa%20Sung%20Shin"> Hwa Sung Shin</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Ischemic stroke means the caused brain damage due to neurological defects, occurring occlusion of cerebral vascular resulting in thrombus or embolism. t-PA (tissue Plasminogen Activator) is the only thrombolytic agent passed the FDA (Food and Drug Administration). However, t-PA directly dissolves the thrombus (direct activity) through fibrinolysis, showing side effects such as re-occlusion. In this study, we evaluated the thrombolytic activities of the serine protease extracted from lugworms inhabiting tidal flats. The new serine protease identified as 38 kDa by SDS-PAGE was not toxic to brain endothelial cells line (hCMEC/D3). Also, the plasmin synthesis inhibition activity (indirect activity) of the new serine protease was confirmed through fibrin zymography assay and fibrin plate assay. It was higher than direct activity as compared to u-PA (urokinase Plasminogen Activator). The activities were found to be maintained at a wide range of temperature (4-70 ℃) and pH 7-10 compared to previous thrombolytic agents from the azocasein assay. In addition, the new serine protease has shown anticoagulant activity from fibrinogenolytic activity assay. In conclusion, the serine protease in lug worms inhabiting the tidal flats could be considered a promising thrombolytic candidate for the treatment of ischemic stroke. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=alkaline%20serine%20protease" title="alkaline serine protease">alkaline serine protease</a>, <a href="https://publications.waset.org/abstracts/search?q=bifunctional%20thrombolytic%20activity" title=" bifunctional thrombolytic activity"> bifunctional thrombolytic activity</a>, <a href="https://publications.waset.org/abstracts/search?q=fibrinolytic%20activity" title=" fibrinolytic activity"> fibrinolytic activity</a>, <a href="https://publications.waset.org/abstracts/search?q=ischemic%20stroke" title=" ischemic stroke"> ischemic stroke</a>, <a href="https://publications.waset.org/abstracts/search?q=lug%20worms" title=" lug worms"> lug worms</a> </p> <a href="https://publications.waset.org/abstracts/75882/a-promising-thrombolytic-and-anticoagulant-serine-protease-purified-from-lug-worms-inhabiting-tidal-flats" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/75882.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">328</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">1095</span> Biological Regulation of Endogenous Enzymatic Activity of Rainbow Trout (Oncorhynchus Mykiss) with Protease Inhibitors Chickpea in Model Systems</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Delgado-Meza%20M.">Delgado-Meza M.</a>, <a href="https://publications.waset.org/abstracts/search?q=Minor-P%C3%A9rez%20H."> Minor-Pérez H.</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Protease is the generic name of enzymes that hydrolyze proteins. These are classified in the subgroup EC3.4.11-99X of the classification enzymes. In food technology the proteolysis is used to modify functional and nutritional properties of food, and in some cases this proteolysis may cause food spoilage. In general, seafood and rainbow trout have accelerated decomposition process once it has done its capture, due to various factors such as the endogenous enzymatic activity that can result in loss of structure, shape and firmness, besides the release of amino acid precursors of biogenic amines. Some studies suggest the use of protease inhibitors from legume as biological regulators of proteolytic activity. The enzyme inhibitors are any substance that reduces the rate of a reaction catalyzed by an enzyme. The objective of this study was to evaluate the reduction of the proteolytic activity of enzymes in extracts of rainbow trout with protease inhibitors obtained from chickpea flour. Different proportions of rainbow trout enzyme extract (75%, 50% and 25%) and extract chickpea enzyme inhibitors were evaluated. Chickpea inhibitors were obtained by mixing 5 g of flour in 30 mL of pH 7.0 phosphate buffer. The sample was centrifuged at 8000 rpm for 10 min. The supernatant was stored at -15°C. Likewise, 20 g of rainbow trout were ground in 20 mL of phosphate buffer solution at pH 7.0 and the mixture was centrifuged at 5000 rpm for 20 min. The supernatant was used for the study. In each treatment was determined the specific enzymatic activity with the technique of Kunitz, using hemoglobin as substrate for the enzymes acid fraction and casein for basic enzymes. Also biuret protein was quantified for each treatment. The results showed for fraction of basic enzymes in the treatments evaluated, that were inhibition of endogenous enzymatic activity. Inhibition values compared to control were 51.05%, 56.59% and 59.29% when the proportions of endogenous enzymes extract rainbow trout were 75%, 50% and 25% and the remaining volume used was extract with inhibitors. Treatments with acid enzymes showed no reduction in enzyme activity. In conclusion chickpea flour reduced the endogenous enzymatic activity of rainbow trout, which may favor its application to increase the half-life of this food. The authors acknowledge the funding provided by the CONACYT for the project 131998. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=rainbouw%20trout" title="rainbouw trout">rainbouw trout</a>, <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=proteolysis" title=" proteolysis"> proteolysis</a>, <a href="https://publications.waset.org/abstracts/search?q=enzyme%20activity" title=" enzyme activity "> enzyme activity </a> </p> <a href="https://publications.waset.org/abstracts/29192/biological-regulation-of-endogenous-enzymatic-activity-of-rainbow-trout-oncorhynchus-mykiss-with-protease-inhibitors-chickpea-in-model-systems" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/29192.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">423</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">1094</span> In Silico Study of Antiviral Drugs Against Three Important Proteins of Sars-Cov-2 Using Molecular Docking Method</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Alireza%20Jalalvand">Alireza Jalalvand</a>, <a href="https://publications.waset.org/abstracts/search?q=Maryam%20Saleh"> Maryam Saleh</a>, <a href="https://publications.waset.org/abstracts/search?q=Somayeh%20Behjat%20Khatouni"> Somayeh Behjat Khatouni</a>, <a href="https://publications.waset.org/abstracts/search?q=Zahra%20Bahri%20Najafi"> Zahra Bahri Najafi</a>, <a href="https://publications.waset.org/abstracts/search?q=Foroozan%20Fatahinia"> Foroozan Fatahinia</a>, <a href="https://publications.waset.org/abstracts/search?q=Narges%20Ismailzadeh"> Narges Ismailzadeh</a>, <a href="https://publications.waset.org/abstracts/search?q=Behrokh%20Farahmand"> Behrokh Farahmand</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Object: In the last two decades, the recent outbreak of Coronavirus (SARS-CoV-2) imposed a global pandemic in the world. Despite the increasing prevalence of the disease, there are no effective drugs to treat it. A suitable and rapid way to afford an effective drug and treat the global pandemic is a computational drug study. This study used molecular docking methods to examine the potential inhibition of over 50 antiviral drugs against three fundamental proteins of SARS-CoV-2. METHODS: Through a literature review, three important proteins (a key protease, RNA-dependent RNA polymerase (RdRp), and spike) were selected as drug targets. Three-dimensional (3D) structures of protease, spike, and RdRP proteins were obtained from the Protein Data Bank. Protein had minimal energy. Over 50 antiviral drugs were considered candidates for protein inhibition and their 3D structures were obtained from drug banks. The Autodock 4.2 software was used to define the molecular docking settings and run the algorithm. RESULTS: Five drugs, including indinavir, lopinavir, saquinavir, nelfinavir, and remdesivir, exhibited the highest inhibitory potency against all three proteins based on the binding energies and drug binding positions deduced from docking and hydrogen-bonding analysis. Conclusions: According to the results, among the drugs mentioned, saquinavir and lopinavir showed the highest inhibitory potency against all three proteins compared to other drugs. It may enter laboratory phase studies as a dual-drug treatment to inhibit SARS-CoV-2. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=covid-19" title="covid-19">covid-19</a>, <a href="https://publications.waset.org/abstracts/search?q=drug%20repositioning" title=" drug repositioning"> drug repositioning</a>, <a href="https://publications.waset.org/abstracts/search?q=molecular%20docking" title=" molecular docking"> molecular docking</a>, <a href="https://publications.waset.org/abstracts/search?q=lopinavir" title=" lopinavir"> lopinavir</a>, <a href="https://publications.waset.org/abstracts/search?q=saquinavir" title=" saquinavir"> saquinavir</a> </p> <a href="https://publications.waset.org/abstracts/165518/in-silico-study-of-antiviral-drugs-against-three-important-proteins-of-sars-cov-2-using-molecular-docking-method" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/165518.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">88</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">1093</span> Production of Fish Hydrolyzates by Single and Multiple Protease Treatments under Medium High Pressure of 300 MPa</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Namsoo%20Kim">Namsoo Kim</a>, <a href="https://publications.waset.org/abstracts/search?q=So-Hee%20Son"> So-Hee Son</a>, <a href="https://publications.waset.org/abstracts/search?q=Jin-Soo%20Maeng"> Jin-Soo Maeng</a>, <a href="https://publications.waset.org/abstracts/search?q=Yong-Jin%20Cho"> Yong-Jin Cho</a>, <a href="https://publications.waset.org/abstracts/search?q=Chong-Tai%20Kim"> Chong-Tai Kim</a> </p> <p class="card-text"><strong>Abstract:</strong></p> It has been reported that some enzymes such as trypsin and Alcalase 2.4L are tolerant to a medium high pressure of 300 MPa and preparation of protein hydrolyzates under 300 MPa was advantageous with regard to hydrolysis rate and thus production yield compared with the counterpart under ambient pressure.1,2) In this study, nine fish comprising halibut, soft shell clam and carp were hydrolyzed using Flavourzyme 500MG only, and the combination of Flavourzyme 500 mg, Alcalase 2.4 L, Marugoto E, and Protamex under 300 MPa. Then, the effects of single and multiple protease treatments were determined with respect to contents of soluble solid (SS) and soluble nitrogen, sensory attributes, electrophoretic profiles, and HPLC peak patterns of the fish hydrolyzates (FHs) from various species. The contents of SS of the FHs were quite species-specific and the hydrolyzates of halibut showed the highest SS contents. At this point, multiple protease treatment increased SS content conspicuously in all fish tested. The contents of total soluble nitrogen and TCA-soluble nitrogen were well correlated with those of SS irrespective of fish species and methods of enzyme treatment. Also, it was noticed that multiple protease treatment improved sensory attributes of the FHs considerably. Electropherograms of the FHs showed fast migrating peptide bands that had the molecular masses mostly lower than 1 kDa and this was confirmed by peptide patterns from HPLC analysis for some FHs that had good sensory quality. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=production" title="production">production</a>, <a href="https://publications.waset.org/abstracts/search?q=fish%20hydrolyzates" title=" fish hydrolyzates"> fish hydrolyzates</a>, <a href="https://publications.waset.org/abstracts/search?q=protease%20treatments" title=" protease treatments"> protease treatments</a>, <a href="https://publications.waset.org/abstracts/search?q=high%20pressure" title=" high pressure"> high pressure</a> </p> <a href="https://publications.waset.org/abstracts/2490/production-of-fish-hydrolyzates-by-single-and-multiple-protease-treatments-under-medium-high-pressure-of-300-mpa" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/2490.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">283</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">1092</span> Towards Designing of a Potential New HIV-1 Protease Inhibitor Using Quantitative Structure-Activity Relationship Study in Combination with Molecular Docking and Molecular Dynamics Simulations</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Mouna%20Baassi">Mouna Baassi</a>, <a href="https://publications.waset.org/abstracts/search?q=Mohamed%20Moussaoui"> Mohamed Moussaoui</a>, <a href="https://publications.waset.org/abstracts/search?q=Hatim%20Soufi"> Hatim Soufi</a>, <a href="https://publications.waset.org/abstracts/search?q=Sanchaita%20RajkhowaI"> Sanchaita RajkhowaI</a>, <a href="https://publications.waset.org/abstracts/search?q=Ashwani%20Sharma"> Ashwani Sharma</a>, <a href="https://publications.waset.org/abstracts/search?q=Subrata%20Sinha"> Subrata Sinha</a>, <a href="https://publications.waset.org/abstracts/search?q=Said%20Belaaouad"> Said Belaaouad</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Human Immunodeficiency Virus type 1 protease (HIV-1 PR) is one of the most challenging targets of antiretroviral therapy used in the treatment of AIDS-infected people. The performance of protease inhibitors (PIs) is limited by the development of protease mutations that can promote resistance to the treatment. The current study was carried out using statistics and bioinformatics tools. A series of thirty-three compounds with known enzymatic inhibitory activities against HIV-1 protease was used in this paper to build a mathematical model relating the structure to the biological activity. These compounds were designed by software; their descriptors were computed using various tools, such as Gaussian, Chem3D, ChemSketch and MarvinSketch. Computational methods generated the best model based on its statistical parameters. The model’s applicability domain (AD) was elaborated. Furthermore, one compound has been proposed as efficient against HIV-1 protease with comparable biological activity to the existing ones; this drug candidate was evaluated using ADMET properties and Lipinski’s rule. Molecular Docking performed on Wild Type and Mutant Type HIV-1 proteases allowed the investigation of the interaction types displayed between the proteases and the ligands, Darunavir (DRV) and the new drug (ND). Molecular dynamics simulation was also used in order to investigate the complexes’ stability, allowing a comparative study of the performance of both ligands (DRV & ND). Our study suggested that the new molecule showed comparable results to that of Darunavir and may be used for further experimental studies. Our study may also be used as a pipeline to search and design new potential inhibitors of HIV-1 proteases. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=QSAR" title="QSAR">QSAR</a>, <a href="https://publications.waset.org/abstracts/search?q=ADMET%20properties" title=" ADMET properties"> ADMET properties</a>, <a href="https://publications.waset.org/abstracts/search?q=molecular%20docking" title=" molecular docking"> molecular docking</a>, <a href="https://publications.waset.org/abstracts/search?q=molecular%20dynamics%20simulation." title=" molecular dynamics simulation."> molecular dynamics simulation.</a> </p> <a href="https://publications.waset.org/abstracts/187453/towards-designing-of-a-potential-new-hiv-1-protease-inhibitor-using-quantitative-structure-activity-relationship-study-in-combination-with-molecular-docking-and-molecular-dynamics-simulations" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/187453.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">38</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">1091</span> Pathological Gambling and Impulsivity: Comparison of the Eight Laboratory Measures of Inhibition Capacities</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Semion%20Kertzman">Semion Kertzman</a>, <a href="https://publications.waset.org/abstracts/search?q=Pinhas%20Dannon"> Pinhas Dannon</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Impulsive behaviour and the underlying brain processes are hypothesized to be central in the development and maintenance of pathological gambling. Inhibition ability can be differentially impaired in pathological gamblers (PGs). Aims: This study aimed to compare the ability of eight widely used inhibition measures to discriminate between PGs and healthy controls (HCs). Methods: PGs (N=51) and demographically matched HCs (N=51) performed cognitive inhibition (the Stroop), motor inhibition (the Go/NoGo) and reflective inhibition (the Matching Familiar Figures (MFFT)) tasks. Results: An augmented total interference response time in the Stroop task (η² =0.054), a large number of commission errors (η² =0.053) in the Go/NoGo task, and the total number of errors in the MFFT (η² =0.05) can discriminate PGs from HCs. Other measures are unable to differentiate between PGs and HCs. No significant correlations were observed between inhibition measures. Conclusion: Inhibition measures varied in the ability to discriminate PGs from HCs. Most inhibition measures were not relevant to gambling behaviour. PGs do not express rash, impulsive behaviour, such as quickly choosing an answer without thinking. In contrast, in PGs, inhibition impairment was related to slow-inaccurate performance. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=pathological%20gambling" title="pathological gambling">pathological gambling</a>, <a href="https://publications.waset.org/abstracts/search?q=impulsivity" title=" impulsivity"> impulsivity</a>, <a href="https://publications.waset.org/abstracts/search?q=neurocognition" title=" neurocognition"> neurocognition</a>, <a href="https://publications.waset.org/abstracts/search?q=addiction" title=" addiction"> addiction</a> </p> <a href="https://publications.waset.org/abstracts/54541/pathological-gambling-and-impulsivity-comparison-of-the-eight-laboratory-measures-of-inhibition-capacities" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/54541.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">302</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">1090</span> Isolation and Identification Fibrinolytic Protease Endophytic Fungi from Hibiscus Leaves in Shah Alam</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Mohd%20Sidek%20Ahmad">Mohd Sidek Ahmad</a>, <a href="https://publications.waset.org/abstracts/search?q=Zainon%20Mohd%20Noor"> Zainon Mohd Noor</a>, <a href="https://publications.waset.org/abstracts/search?q=Zaidah%20Zainal%20Ariffin"> Zaidah Zainal Ariffin</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Fibrin degradation is an important part in prevention or treatment of intravascular thrombosis and cardiovascular diseases. Plasmin like fibrinolytic enzymes has given new hope to patient with cardiovascular diseases by treating fibrin aggregation related diseases with traditional plasminogen activator which have many side effects. Various researches involving wide range of sources for production of fibrinolytic proteases, from bacteria, fungi, insects and fermented foods. But few have looked into endophytic fungi as a potential source. Sixteen (16) endophytic fungi were isolated from Hibiscus sp. leaves from six different locations in Shah Alam, Selangor. Only two endophytic fungi, FH3 and S13 showed positive fibrinolytic protease activities. FH3 produced 5.78cm and S13 produced 4.48cm on Skim Milk Agar after 4 days of incubation at 27°C. Fibrinolytic activity was observed; 3.87cm and 1.82cm diameter clear zone on fibrin plate of FH3 and S13 respectively. 18srRNA was done for identification of the isolated fungi with positive fibrinolytic protease. S13 had the highest similarity (100%) to that of Penicillium citrinum strain TG2 and FH3 had the highest similarity (99%) to that of Fusarium sp. FW2PhC1, Fusarium sp. 13002, Fusarium sp. 08006, Fusarium equiseti strain Salicorn 8 and Fungal sp. FCASAn-2. Media composition variation showed the effects of carbon nitrogen on protein concentration, where the decrement of 50% of media composition caused drastic decrease in protease of FH3 from 1.081 to 0.056 and also S13 from 2.946 to 0.198. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=isolation" title="isolation">isolation</a>, <a href="https://publications.waset.org/abstracts/search?q=identification" title=" identification"> identification</a>, <a href="https://publications.waset.org/abstracts/search?q=fibrinolytic%20protease" title=" fibrinolytic protease"> fibrinolytic protease</a>, <a href="https://publications.waset.org/abstracts/search?q=endophytic%20fungi" title=" endophytic fungi"> endophytic fungi</a>, <a href="https://publications.waset.org/abstracts/search?q=Hibiscus%20leaves" title=" Hibiscus leaves"> Hibiscus leaves</a> </p> <a href="https://publications.waset.org/abstracts/15095/isolation-and-identification-fibrinolytic-protease-endophytic-fungi-from-hibiscus-leaves-in-shah-alam" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/15095.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">432</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">1089</span> Enzyme Producing Psyhrophilic Pseudomonas app. Isolated from Poultry Meats</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Ali%20Aydin">Ali Aydin</a>, <a href="https://publications.waset.org/abstracts/search?q=Mert%20Sudagidan"> Mert Sudagidan</a>, <a href="https://publications.waset.org/abstracts/search?q=Aysen%20Coban"> Aysen Coban</a>, <a href="https://publications.waset.org/abstracts/search?q=Alparslan%20Kadir%20Devrim"> Alparslan Kadir Devrim </a> </p> <p class="card-text"><strong>Abstract:</strong></p> Pseudomonas spp. (specifically, P. fluorescens and P. fragi) are considered the principal spoilage microorganisms of refrigerated poultry meats. The higher the level psychrophilic spoilage Pseudomonas spp. on carcasses at the end of processing lead to decrease the shelf life of the refrigerated product. The aim of the study was the identification of psychrophilic Pseudomonas spp. having proteolytic and lipolytic activities from poultry meats by 16S rRNA and rpoB gene sequencing, investigation of protease and lipase related genes and determination of proteolytic activity of Pseudomonas spp. In the of isolation procedure, collected chicken meat samples from local markets and slaughterhouses were homogenized and the lysates were incubated on Standard method agar and Skim Milk agar for selection of proteolytic bacteria and tributyrin agar for selection of lipolytic bacteria at +4 °C for 7 days. After detection of proteolytic and lipolytic colonies, the isolates were firstly analyzed by biochemical tests such as Gram staining, catalase and oxidase tests. DNA gene sequencing analysis and comparison with GenBank revealed that 126 strong enzyme Pseudomonas spp. were identified as predominantly P. fluorescens (n=55), P. fragi (n=42), Pseudomonas spp. (n=24), P. cedrina (n=2), P. poae (n=1), P. koreensis (n=1), and P. gessardi (n=1). Additionally, protease related aprX gene was screened in the strains and it was detected in 69/126 strains, whereas, lipase related lipA gene was found in 9 Pseudomonas strains. Protease activity was determined using commercially available protease assay kit and 5 strains showed high protease activity. The results showed that psychrophilic Pseudomonas strains were present in chicken meat samples and they can produce important levels of proteases and lipases for food spoilage to decrease food quality and safety. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=Pseudomonas" title="Pseudomonas">Pseudomonas</a>, <a href="https://publications.waset.org/abstracts/search?q=chicken%20meat" title=" chicken meat"> chicken meat</a>, <a href="https://publications.waset.org/abstracts/search?q=protease" title=" protease"> protease</a>, <a href="https://publications.waset.org/abstracts/search?q=lipase" title=" lipase"> lipase</a> </p> <a href="https://publications.waset.org/abstracts/31581/enzyme-producing-psyhrophilic-pseudomonas-app-isolated-from-poultry-meats" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/31581.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">387</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">1088</span> Bacillus thuringiensis CHGP12 Uses a Multifaceted Strategy to Suppress Fusarium Wilt of Chickpea and to Enhance the Total Biomass of Chickpea Plants</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Muhammad%20Naveed%20Aslam">Muhammad Naveed Aslam</a>, <a href="https://publications.waset.org/abstracts/search?q=Rida%20Fatima"> Rida Fatima</a>, <a href="https://publications.waset.org/abstracts/search?q=Anam%20Moosa"> Anam Moosa</a>, <a href="https://publications.waset.org/abstracts/search?q=Muhammad%20Taimoor%20Shakeel"> Muhammad Taimoor Shakeel</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Bacillus strains produce antifungal secondary metabolites making them potential candidates for suppressing Fusarium wilt of chickpea disease. In this study, eighteen Bacillus strains were evaluated for their antagonistic effect against Fusarium oxysporum f. sp. ciceris causing Fusarium wilt of chickpea disease. In a direct antifungal assay, thirteen strains showed significant inhibition zones while the remaining five strains did not produce inhibition zones of FOC. Bacillus thuringiensis CHGP12 was the most promising strain exhibiting the highest inhibition of FOC. Antifungal lipopeptides were extracted from CHGP12 strain which showed significant inhibition of the pathogen. Liquid chromatography mass spectrometry (LCMS) analysis revealed that CHGP12 was positive for the presence of iturin, fengycin, surfactin, bacillaene, bacillibactin, plantazolicin, and bacilysin. CHGP12 was tested for biochemical determinants in an in vitro qualitative test where it showed the ability to produce lipase, amylase, cellulase, protease, siderophores, and indole 3-acetic acid (IAA). Furthermore, in a greenhouse experiment CHGP12 also showed a significant decrease in the disease severity in treated plants compared to control. Moreover, CHGP12 also exhibited a significant increase in plant growth parameters viz, root and shoot growth parameters, stomatal conductance, and photosynthesis rate. Conclusively, our findings present the promising potential of Bacillus strain CHGP12 to suppress Fusarium wilt of chickpea and to promote plant growth. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=liquid%20chromatography%20mass%20spectrometry" title="liquid chromatography mass spectrometry">liquid chromatography mass spectrometry</a>, <a href="https://publications.waset.org/abstracts/search?q=growth%20promotion" title=" growth promotion"> growth promotion</a>, <a href="https://publications.waset.org/abstracts/search?q=antagonism" title=" antagonism"> antagonism</a>, <a href="https://publications.waset.org/abstracts/search?q=hydrolytic%20enzymes" title=" hydrolytic enzymes"> hydrolytic enzymes</a>, <a href="https://publications.waset.org/abstracts/search?q=inhibition" title=" inhibition"> inhibition</a>, <a href="https://publications.waset.org/abstracts/search?q=lipopeptides." title=" lipopeptides."> lipopeptides.</a> </p> <a href="https://publications.waset.org/abstracts/158702/bacillus-thuringiensis-chgp12-uses-a-multifaceted-strategy-to-suppress-fusarium-wilt-of-chickpea-and-to-enhance-the-total-biomass-of-chickpea-plants" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/158702.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">135</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">1087</span> Production of Organic Solvent Tolerant Hydrolytic Enzymes (Amylase and Protease) by Bacteria Isolated from Soil of a Dairy Farm</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Alok%20Kumar">Alok Kumar</a>, <a href="https://publications.waset.org/abstracts/search?q=Hari%20Ram"> Hari Ram</a>, <a href="https://publications.waset.org/abstracts/search?q=Lebin%20Thomas"> Lebin Thomas</a>, <a href="https://publications.waset.org/abstracts/search?q=Ved%20Pal%20Singh"> Ved Pal Singh</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Organic solvent tolerant amylases and proteases of microbial origin are in great demand for their application in transglycosylation of water-insoluble flavanoids and in peptide synthesizing reaction in organic media. Most of the amylases and proteases are unstable in presence of organic solvent. In the present work two different bacterial strains M-11 and VP-07 were isolated from the soil sample of a dairy farm in Delhi, India, for the efficient production of extracellular amylase and protease through their screening on starch agar (SA) and skimmed milk agar (SMA) plates, respectively. Both the strains (M-11 and VP-07) were identified based on morphological, biochemical and 16S rRNA gene sequencing methods. After analysis through Ez-Taxon software, the strains M-11 and VP-07 were found to have maximum pairwise similarity of 98.63% and 100% with Bacillus subtilis subsp. inaquosorum BGSC 3A28 and Bacillus anthracis ATCC 14578 and were therefore identified as Bacillus sp. UKS1 and Bacillus sp. UKS2, respectively. Time course study of enzyme activity and bacterial growth has shown that both strains exhibited typical sigmoid growth behavior and maximum production of amylase (180 U/ml) and protease (78 U/ml) by these strains (UKS1 and UKS2) was commenced during stationary phase of growth at 24 and 20 h, respectively. Thereafter, both amylase and protease were tested for their tolerance towards organic solvents and were found to be active as well stable in p-xylene (130% and 115%), chloroform (110% and 112%), isooctane (119% and 107%), benzene (121% and 104%), n-hexane (116% and 103%) and toluene (112% and 101%, respectively). Owing to such properties, these enzymes can be exploited for their potential application in industries for organic synthesis. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=amylase" title="amylase">amylase</a>, <a href="https://publications.waset.org/abstracts/search?q=enzyme%20activity" title=" enzyme activity"> enzyme activity</a>, <a href="https://publications.waset.org/abstracts/search?q=industrial%20applications" title=" industrial applications"> industrial applications</a>, <a href="https://publications.waset.org/abstracts/search?q=organic%20solvent%20tolerant" title=" organic solvent tolerant"> organic solvent tolerant</a>, <a href="https://publications.waset.org/abstracts/search?q=protease" title=" protease"> protease</a> </p> <a href="https://publications.waset.org/abstracts/4042/production-of-organic-solvent-tolerant-hydrolytic-enzymes-amylase-and-protease-by-bacteria-isolated-from-soil-of-a-dairy-farm" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/4042.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">343</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">1086</span> The Hidden Mechanism beyond Ginger (Zingiber officinale Rosc.) Potent in vivo and in vitro Anti-Inflammatory Activity</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Shahira%20M.%20Ezzat">Shahira M. Ezzat</a>, <a href="https://publications.waset.org/abstracts/search?q=Marwa%20I.%20Ezzat"> Marwa I. Ezzat</a>, <a href="https://publications.waset.org/abstracts/search?q=Mona%20M.%20Okba"> Mona M. Okba</a>, <a href="https://publications.waset.org/abstracts/search?q=Esther%20T.%20Menze"> Esther T. Menze</a>, <a href="https://publications.waset.org/abstracts/search?q=Ashraf%20B.%20Abdel-Naim"> Ashraf B. Abdel-Naim</a>, <a href="https://publications.waset.org/abstracts/search?q=Shahnas%20O.%20Mohamed"> Shahnas O. Mohamed</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Background: In order to decrease the burden of the high cost of synthetic drugs, it is important to focus on phytopharmaceuticals. The aim of our study was to search for the mechanism of ginger (Zingiber officinale Roscoe) anti-inflammatory potential and to correlate it to its biophytochemicals. Methods: Various extracts viz. water, 50%, 70%, 80%, and 90% ethanol were prepared from ginger rhizomes. Fractionation of the aqueous extract (AE) was accomplished using Diaion HP-20. In vitro anti-inflammatory activity of the different extracts and isolated compounds was evaluated by protein denaturation inhibition, membrane stabilization, protease inhibition, and anti-lipoxygenase assays. In vivo anti-inflammatory activity of AE was estimated by assessment of rat paw oedema after carrageenan injection. Prostaglandin E2 (PGE2), certain inflammation markers (TNF-α, IL-6, IL-1α, IL-1β, INFr, MCP-1MIP, RANTES, and Nox) levels and MPO activity in the paw edema exudates were measured. Total antioxidant capacity (TAC) was also determined. Histopathological alterations of paw tissues were scored. Results: All the tested extracts showed significant (p < 0.1) anti-inflammatory activities. The highest percentage of heat induced albumin denaturation (66%) was exhibited by the 50% ethanol (250 μg/ml). The 70 and 90% ethanol extracts (500 μg/ml) were more potent as membrane stabilizers (34.5 and 37%, respectively) than diclofenac (33%). The 80 and 90% ethanol extracts (500 μg/ml) showed maximum protease inhibition (56%). The strongest anti-lipoxygenase activity was observed for the AE. It showed more significant lipoxygenase inhibition activity than that of diclofenac (58% and 52%, respectively) at the same concentration (125 μg/ml). Fractionation of AE yielded four main fractions (Fr I-IV) which showed significant in vitro anti-inflammatory. Purification of Fr-III and IV led to the isolation of 6-poradol (G1), 6-shogaol (G2); methyl 6- gingerol (G3), 5-gingerol (G4), 6-gingerol (G5), 8-gingerol (G6), 10-gingerol (G7), and 1-dehydro-6-gingerol (G8). G2 (62.5 ug/ml), G1 (250 ug/ml), and G8 (250 ug/ml) exhibited potent anti-inflammatory activity in all studied assays, while G4 and G5 exhibited moderate activity. In vivo administration of AE ameliorated rat paw oedema in a dose-dependent manner. AE (at 200 mg/kg) showed significant reduction (60%) of PGE2 production. The AE at different doses (at 25-200 mg/kg) showed significant reduction in inflammatory markers except for IL-1α. AE (at 25 mg/kg) is superior to indomethacin in reduction of IL-1β. Treatment of animals with the AE (100, 200 mg/kg) or indomethacin (10 mg/kg) showed significant reduction in TNF-α, IL-6, MCP-1, and RANTES levels, and MPO activity by about (31, 57 and 32% ) (65, 60 and 57%) (27, 41 and 28%) (23, 32 and 23%) (66, 67 and 67%) respectively. AE at 100 and 200 mg/kg was equipotent to indomethacin in reduction of NOₓ level and in increasing the TAC. Histopathological examination revealed very few inflammatory cells infiltration and oedema after administration of AE (200 mg/kg) prior to carrageenan. Conclusion: Ginger anti-inflammatory activity is mediated by inhibiting macrophage and neutrophils activation as well as negatively affecting monocyte and leukocyte migration. Moreover, it produced dose-dependent decrease in pro-inflammatory cytokines and chemokines and replenished the total antioxidant capacity. We strongly recommend future investigations of ginger in the potential signal transduction pathways. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=anti-lipoxygenase%20activity" title="anti-lipoxygenase activity">anti-lipoxygenase activity</a>, <a href="https://publications.waset.org/abstracts/search?q=inflammatory%20markers" title=" inflammatory markers"> inflammatory markers</a>, <a href="https://publications.waset.org/abstracts/search?q=1-dehydro-6-gingerol" title=" 1-dehydro-6-gingerol"> 1-dehydro-6-gingerol</a>, <a href="https://publications.waset.org/abstracts/search?q=6-shogaol" title=" 6-shogaol"> 6-shogaol</a> </p> <a href="https://publications.waset.org/abstracts/74482/the-hidden-mechanism-beyond-ginger-zingiber-officinale-rosc-potent-in-vivo-and-in-vitro-anti-inflammatory-activity" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/74482.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">252</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">1085</span> Contribution of Artificial Intelligence in the Studies of Natural Compounds Against SARS-COV-2</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Salah%20Belaidi">Salah Belaidi</a> </p> <p class="card-text"><strong>Abstract:</strong></p> We have carried out extensive and in-depth research to search for bioactive compounds based on Algerian plants. A selection of 50 ligands from Algerian medicinal plants. Several compounds used in herbal medicine have been drawn using Marvin Sketch software. We determined the three-dimensional structures of the ligands with the MMFF94 force field in order to prepare these ligands for molecular docking. The 3D protein structure of the SARS-CoV-2 main protease was taken from the Protein Data Bank. We used AutoDockVina software to apply molecular docking. The hydrogen atoms were added during the molecular docking process, and all the twist bonds of the ligands were added using the (ligand) module in the AutoDock software. The COVID-19 main protease (Mpro) is a key enzyme that plays a vital role in viral transcription and mediating replication, so it is a very attractive drug target for SARS-CoV-2. In this work, an evaluation was carried out on the biologically active compounds present in these selected medicinal plants as effective inhibitors of the protease enzyme of COVID-19, with an in-depth computational calculation of the molecular docking using the Autodock Vina software. The top 7 ligands: Phloroglucinol, Afzelin, Myricetin-3-O- rutinosidTricin 7-neohesperidoside, Silybin, Silychristinthat and Kaempferol are selected among the 50 molecules studied which are Algerian medicinal plants, whose selection is based on the best binding energy which is relatively low compared to the reference molecule with binding affinities of -9.3, -9.3, -9, -8.9, -8 .5, 8.3 and -8.3 kcal mol-1 respectively. Then, we analyzed the ADME properties of the best7 ligands using the web server SwissADME. Two ligands (Silybin, Silychristin) were found to be potential candidates for the discovery and design of novel drug inhibitors of the protease enzyme of SARS-CoV-2. The stability of the two ligands in complexing with the Mpro protease was validated by molecular dynamics simulation; they revealed a stable trajectory in both techniques, RMSD and RMSF, by showing molecular properties with coherent interactions in molecular dynamics simulations. Finally, we conclude that the Silybin ligand forms a more stable complex with the Mpro protease compared to the Silychristin ligand. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=COVID-19" title="COVID-19">COVID-19</a>, <a href="https://publications.waset.org/abstracts/search?q=medicinal%20plants" title=" medicinal plants"> medicinal plants</a>, <a href="https://publications.waset.org/abstracts/search?q=molecular%20docking" title=" molecular docking"> molecular docking</a>, <a href="https://publications.waset.org/abstracts/search?q=ADME%20properties" title=" ADME properties"> ADME properties</a>, <a href="https://publications.waset.org/abstracts/search?q=molecular%20dynamics" title=" molecular dynamics"> molecular dynamics</a> </p> <a href="https://publications.waset.org/abstracts/188747/contribution-of-artificial-intelligence-in-the-studies-of-natural-compounds-against-sars-cov-2" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/188747.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">34</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">1084</span> Human LACE1 Functions Pro-Apoptotic and Interacts with Mitochondrial YME1L Protease</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Lukas%20Stiburek">Lukas Stiburek</a>, <a href="https://publications.waset.org/abstracts/search?q=Jana%20Cesnekova"> Jana Cesnekova</a>, <a href="https://publications.waset.org/abstracts/search?q=Josef%20Houstek"> Josef Houstek</a>, <a href="https://publications.waset.org/abstracts/search?q=Jiri%20Zeman"> Jiri Zeman</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Cellular function depends on mitochondrial function and integrity that is therefore maintained by several classes of proteins possessing chaperone and/or proteolytic activities. In this work, we focused on characterization of LACE1 (lactation elevated 1) function in mitochondrial protein homeostasis maintenance. LACE1 is the human homologue of yeast mitochondrial Afg1 ATPase, a member of SEC18-NSF, PAS1, CDC48-VCP, TBP family. Yeast Afg1 was shown to be involved in mitochondrial complex IV biogenesis, and based on its similarity with CDC48 (p97/VCP) it was suggested to facilitate extraction of polytopic membrane proteins. Here we show that LACE1, which is a mitochondrial integral membrane protein, exists as part of three complexes of approx. 140, 400 and 500 kDa and is essential for maintenance of fused mitochondrial reticulum and lamellar cristae morphology. Using affinity purification of LACE1-FLAG expressed in LACE1 knockdown background we show that the protein physically interacts with mitochondrial inner membrane protease YME1L. We further show that human LACE1 exhibits significant pro-apoptotic activity and that the protein is required for normal function of the mitochondrial respiratory chain. Thus, our work establishes LACE1 as a novel factor with the crucial role in mitochondrial homeostasis maintenance. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=LACE1" title="LACE1">LACE1</a>, <a href="https://publications.waset.org/abstracts/search?q=mitochondria" title=" mitochondria"> mitochondria</a>, <a href="https://publications.waset.org/abstracts/search?q=apoptosis" title=" apoptosis"> apoptosis</a>, <a href="https://publications.waset.org/abstracts/search?q=protease" title=" protease"> protease</a> </p> <a href="https://publications.waset.org/abstracts/46195/human-lace1-functions-pro-apoptotic-and-interacts-with-mitochondrial-yme1l-protease" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/46195.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">312</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">1083</span> Bioactivity of Local Isolated Probiotic to Inhibiting Important Bacterial Pathogens in Aquaculture </h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Abhichet%20Nobhiwong">Abhichet Nobhiwong</a>, <a href="https://publications.waset.org/abstracts/search?q=Jiraporn%20Rojtinnakorn"> Jiraporn Rojtinnakorn</a>, <a href="https://publications.waset.org/abstracts/search?q=Udomluk%20Sompong"> Udomluk Sompong</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Six probiotic strains isolated from Chiang Mai and Chiang Rai province, Thailand; CR1-2, CM3-4, CM5-2, CR7-8, CM10-5 and CM10-8 were used to study their morphology and inhibition activity on three pathogenic bacteria; Aeromonas sp., Streptococcus sp. and Flavobacterium sp. that isolated from infected Nile tilapia. The agar well diffusion technique was applied for 24 and 48 hours incubation. Interestingly, some probiotics showed good inhibition activity both 24 and 48 hours on each 3 bacterial pathogens. The capable inhibiting Aeromonas sp. were CR1-2 and CR5-2 with inhibition diameters of 13.0 mm and 11.2 mm, respectively. For Streptococcus sp., effective probiotics were CR10-2 with inhibition diameters of 10.7 mm. Whereas for Flavobacterium sp., effective probiotics were CR5-2 with inhibition diameter of 9.7 mm. It can be concluded that these probiotics have potentiality to develop as the pathogens biocontrol products. These will be support for safety and organic aquaculture that which the most worthy for people health. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=probiotics" title="probiotics">probiotics</a>, <a href="https://publications.waset.org/abstracts/search?q=Aeromanas%20sp." title=" Aeromanas sp."> Aeromanas sp.</a>, <a href="https://publications.waset.org/abstracts/search?q=Streptococcus%20sp." title=" Streptococcus sp."> Streptococcus sp.</a>, <a href="https://publications.waset.org/abstracts/search?q=Flavobacterium%20sp." title=" Flavobacterium sp."> Flavobacterium sp.</a> </p> <a href="https://publications.waset.org/abstracts/64898/bioactivity-of-local-isolated-probiotic-to-inhibiting-important-bacterial-pathogens-in-aquaculture" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/64898.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">273</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">1082</span> Immunosupressive Effect of Chloroquine through the Inhibition of Myeloperoxidase</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=J.%20B.%20Minari">J. B. Minari</a>, <a href="https://publications.waset.org/abstracts/search?q=O.%20B.%20Oloyede"> O. B. Oloyede</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Polymorphonuclear neutrophils (PMNs) play a crucial role in a variety of infections caused by bacteria, fungi, and parasites. Indeed, the involvement of PMNs in host defence against Plasmodium falciparum is well documented both in vitro and in vivo. Many of the antimalarial drugs such as chloroquine used in the treatment of human malaria significantly reduce the immune response of the host in vitro and in vivo. Myeloperoxidase is the most abundant enzyme found in the polymorphonuclear neutrophil which plays a crucial role in its function. This study was carried out to investigate the effect of chloroquine on the enzyme. In investigating the effects of the drug on myeloperoxidase, the influence of concentration, pH, partition ratio estimation and kinetics of inhibition were studied. This study showed that chloroquine is concentration-dependent inhibitor of myeloperoxidase with an IC50 of 0.03 mM. Partition ratio estimation showed that 40 enzymatic turnover cycles are required for complete inhibition of myeloperoxidase in the presence of chloroquine. The influence of pH on the effect of chloroquine on the enzyme showed significant inhibition of myeloperoxidase at physiological pH. The kinetic inhibition studies showed that chloroquine caused a non-competitive inhibition with an inhibition constant Ki of 0.27mM. The results obtained from this study shows that chloroquine is a potent inhibitor of myeloperoxidase and it is capable of inactivating the enzyme. It is therefore considered that the inhibition of myeloperoxidase in the presence of chloroquine as revealed in this study may partly explain the impairment of polymorphonuclear neutrophil and consequent immunosuppression of the host defence system against secondary infections. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=myeloperoxidase" title="myeloperoxidase">myeloperoxidase</a>, <a href="https://publications.waset.org/abstracts/search?q=chloroquine" title=" chloroquine"> chloroquine</a>, <a href="https://publications.waset.org/abstracts/search?q=inhibition" title=" inhibition"> inhibition</a>, <a href="https://publications.waset.org/abstracts/search?q=neutrophil" title=" neutrophil"> neutrophil</a>, <a href="https://publications.waset.org/abstracts/search?q=immune" title=" immune"> immune</a> </p> <a href="https://publications.waset.org/abstracts/7033/immunosupressive-effect-of-chloroquine-through-the-inhibition-of-myeloperoxidase" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/7033.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">374</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">1081</span> The Equality Test of Ceftriaxone Anti-Bacterial Effect and Ethanol Extract of Ant Plant (Myermecodia pendens Merr. and L. M Perry) to MRSA </h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Rifa%E2%80%99ah%20Mahmudah%20Bulu%E2%80%99">Rifa’ah Mahmudah Bulu’ </a> </p> <p class="card-text"><strong>Abstract:</strong></p> MRSA is an important nosocomial pathogen in the world. Therefore, the prevention and effort to control MRSA is still very important to conduct. One of the preventions of MRSA, which have been reported by several studies, is Cefriaxone and Ethanol Extract of Ant Plant. This research is an experimental test to determine the potency of MRSA’s anti-bacterial with Cefriaxone (30 μg) and Ethanol Extract of Ant Plant (13 mg/ml) based on inhibition zone on LAB (Lempeng Agar Biasa). The size of inhibition zone that is formed on Cefriaxone is adjusted with CSLI criteria, which ≥ 21 mm of inhibition zone is called sensitive; ≤13 mm is called resistance and between 14-20 mm is called intermediate. This research is conducted three times. Comparative test between Cefriaxone and Ethanol Extract of Ant Plant is analyzed by Maan Whitney’s statistic method. The Result of Cefriaxone anti-bacterial potency shows the variety of inhibition zone. Cefriaxone forms approximately 16,5-20 mm with average 18,22mm of inhibition zone that make Cefriaxone’s criteria to MRSA’s inhibition is intermediate. Anti-bacterial potency of Ethanol Extract of Ant Plant is about 0,5-2 mm with average 1,17 mm of inhibition zone that prove MRSA is sensitive to Ant Plant. The conclusion of this research shows that Cefriaxone is intermediate to MRSA’s inhibition, while MRSA is sensitive to Ethanol Extract of Ant Plant, which at the end; it creates different potency of anti-bacterial between Cefriaxone and Ethanol Extract of Ant Plant. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=MRSA" title="MRSA">MRSA</a>, <a href="https://publications.waset.org/abstracts/search?q=cefriaxone" title=" cefriaxone"> cefriaxone</a>, <a href="https://publications.waset.org/abstracts/search?q=ant%20plant" title=" ant plant"> ant plant</a>, <a href="https://publications.waset.org/abstracts/search?q=CSLI" title=" CSLI"> CSLI</a>, <a href="https://publications.waset.org/abstracts/search?q=mann%20whitney" title=" mann whitney"> mann whitney</a> </p> <a href="https://publications.waset.org/abstracts/39334/the-equality-test-of-ceftriaxone-anti-bacterial-effect-and-ethanol-extract-of-ant-plant-myermecodia-pendens-merr-and-l-m-perry-to-mrsa" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/39334.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">367</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">1080</span> Improving the Quality of Casava Peel-Leaf Mixture through Fermentation with Rhizopus oligosporusas Poultry Ration</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Mirnawati">Mirnawati</a>, <a href="https://publications.waset.org/abstracts/search?q=G.%20Ciptaan"> G. Ciptaan</a>, <a href="https://publications.waset.org/abstracts/search?q=Ferawati"> Ferawati</a> </p> <p class="card-text"><strong>Abstract:</strong></p> This study aims to improve the quality of the cassava peel-leaf mixture (CPLM) through fermentation with Rhizopus oligosporusas poultry ration. This research is an experimental study using a completely randomized design (CRD) with four treatments and five replications. The treatments were cassava peel-leaf mixture (CPLM) fermented with Rhizopus oligosporus. The treatments were a combination of cassava peel and leaves with the ratio of; A (9:1), B (8:2), C (7:3), and D (6:4). The observed variables were protease enzyme activity, crude protein, crude fiber, nitrogen retention, digestibility of crude fiber, and metabolic energy. The results of the diversity analysis showed that there was a very significant (p < 0.01) effect on protease activity, crude protein, crude fiber, nitrogen retention, digestibility of crude fiber, and energy metabolism of fermented CPLM. Based on the results of the study, it can be concluded that CPLM (6:4) fermented with Rhizopus oligosporus gave the best results seen from protease activity 7,25 U/ml, 21.23% crude protein, 19.80% crude fiber, 59.65% nitrogen retention, 62.99% crude fiber digestibility and metabolic energy 2671 Kcal/kg. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=quality" title="quality">quality</a>, <a href="https://publications.waset.org/abstracts/search?q=Casava%20peel-leaf%20mixture" title=" Casava peel-leaf mixture"> Casava peel-leaf mixture</a>, <a href="https://publications.waset.org/abstracts/search?q=fermentation" title=" fermentation"> fermentation</a>, <a href="https://publications.waset.org/abstracts/search?q=Rhizopus%20oligosporus" title=" Rhizopus oligosporus"> Rhizopus oligosporus</a> </p> <a href="https://publications.waset.org/abstracts/141172/improving-the-quality-of-casava-peel-leaf-mixture-through-fermentation-with-rhizopus-oligosporusas-poultry-ration" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/141172.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">185</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">1079</span> Evaluation of the Analgesic Activity of Defatted Methanol Extract of Capparis spinosa L. Root Barks</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Asma%20Meddour">Asma Meddour</a>, <a href="https://publications.waset.org/abstracts/search?q=Mouloud%20Yahia"> Mouloud Yahia</a>, <a href="https://publications.waset.org/abstracts/search?q=Afaf%20Benhouda"> Afaf Benhouda</a>, <a href="https://publications.waset.org/abstracts/search?q=Souhila%20Benbia"> Souhila Benbia</a>, <a href="https://publications.waset.org/abstracts/search?q=Hachani%20Khadhraoui"> Hachani Khadhraoui</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Peripheral analgesic activity of defatted methanol extract of root barks of Capparis spinosa was tested orally at the dose of 100 and 200 mg/kg against pain induced by acetic acid in rats. The dose of 200 mg/kg presents significant analgesic effect with a percentage of inhibition of torsions of 88.51% compared to the positive control which is the acetylsalicylic acid which represents a percentage of inhibition of 92.55%. The dose of 100 mg/kg presents a percentage of inhibition of 81.68%. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=peripheral%20analgesic%20activity" title="peripheral analgesic activity">peripheral analgesic activity</a>, <a href="https://publications.waset.org/abstracts/search?q=Capparis%20spinosa" title=" Capparis spinosa"> Capparis spinosa</a>, <a href="https://publications.waset.org/abstracts/search?q=percentage%20of%20inhibition%20of%20torsions" title=" percentage of inhibition of torsions"> percentage of inhibition of torsions</a>, <a href="https://publications.waset.org/abstracts/search?q=chemical%20sciences" title=" chemical sciences"> chemical sciences</a> </p> <a href="https://publications.waset.org/abstracts/6423/evaluation-of-the-analgesic-activity-of-defatted-methanol-extract-of-capparis-spinosa-l-root-barks" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/6423.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">295</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">1078</span> Downhole Corrosion Inhibition Treatment for Water Supply Wells</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Nayif%20Alrasheedi">Nayif Alrasheedi</a>, <a href="https://publications.waset.org/abstracts/search?q=Sultan%20Almutairi"> Sultan Almutairi</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Field-wide, a water supply wells’ downhole corrosion inhibition program is being applied to maintain downhole component integrity and keep the fluid corrosivity below 5 MPY. Batch treatment is currently used to inject the oil field chemical. This work is a case study consisting of analytical procedures used to optimize the frequency of the good corrosion inhibition treatments. During the study, a corrosion cell was fitted with a special three-electrode configuration for electrochemical measurements, electrochemical linear polarization, corrosion monitoring, and microbial analysis. This study revealed that the current practice is not able to mitigate material corrosion in the downhole system for more than three months. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=downhole%20corrosion%20inhibition" title="downhole corrosion inhibition">downhole corrosion inhibition</a>, <a href="https://publications.waset.org/abstracts/search?q=electrochemical%20measurements" title=" electrochemical measurements"> electrochemical measurements</a>, <a href="https://publications.waset.org/abstracts/search?q=electrochemical%20linear%20polarization" title=" electrochemical linear polarization"> electrochemical linear polarization</a>, <a href="https://publications.waset.org/abstracts/search?q=corrosion%20monitoring" title=" corrosion monitoring"> corrosion monitoring</a> </p> <a href="https://publications.waset.org/abstracts/150495/downhole-corrosion-inhibition-treatment-for-water-supply-wells" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/150495.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">182</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">1077</span> Aqueous Extract of Argemone Mexicana Roots for Effective Corrosion Inhibition of Mild Steel in HCl Environment </h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Gopal%20Ji">Gopal Ji</a>, <a href="https://publications.waset.org/abstracts/search?q=Priyanka%20Dwivedi"> Priyanka Dwivedi</a>, <a href="https://publications.waset.org/abstracts/search?q=Shanthi%20Sundaram"> Shanthi Sundaram</a>, <a href="https://publications.waset.org/abstracts/search?q=Rajiv%20Prakash"> Rajiv Prakash</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Inhibition effect of aqueous Argemone Mexicana root extract (AMRE) on mild steel corrosion in 1 M HCl has been studied by weight loss, Tafel polarization curves, electrochemical impedance spectroscopy (EIS), scanning electron microscopy (SEM) and atomic force microscopy (AFM) techniques. Results indicate that inhibition ability of AMRE increases with the increasing amount of the extract. A maximum corrosion inhibition of 94% is acknowledged at the extract concentration of 400 mg L-1. Polarization curves and impedance spectra reveal that both cathodic and anodic reactions are suppressed due to passive layer formation at metal-acid interface. It is also confirmed by SEM micro graphs and FTIR studies. Furthermore, the effects of acid concentration (1-5 M), immersion time (120 hours) and temperature (30-60˚C) on inhibition potential of AMRE have been investigated by weight loss method and electrochemical techniques. Adsorption mechanism is also proposed on the basis of weight loss results, which shows good agreement with Langmuir isotherm. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=mild%20steel" title="mild steel">mild steel</a>, <a href="https://publications.waset.org/abstracts/search?q=polarization" title=" polarization"> polarization</a>, <a href="https://publications.waset.org/abstracts/search?q=SEM" title=" SEM"> SEM</a>, <a href="https://publications.waset.org/abstracts/search?q=acid%20corrosion" title=" acid corrosion"> acid corrosion</a>, <a href="https://publications.waset.org/abstracts/search?q=EIS" title=" EIS"> EIS</a>, <a href="https://publications.waset.org/abstracts/search?q=green%20inhibition" title=" green inhibition"> green inhibition</a> </p> <a href="https://publications.waset.org/abstracts/15600/aqueous-extract-of-argemone-mexicana-roots-for-effective-corrosion-inhibition-of-mild-steel-in-hcl-environment" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/15600.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">491</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">1076</span> Activation of AMPK-TSC axis is involved in cryptotanshinone inhibition of mTOR signaling in cancer cells </h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Wenxing%20Chen">Wenxing Chen</a>, <a href="https://publications.waset.org/abstracts/search?q=Guangying%20Chen"> Guangying Chen</a>, <a href="https://publications.waset.org/abstracts/search?q=Yin%20Lu"> Yin Lu</a>, <a href="https://publications.waset.org/abstracts/search?q=Shile%20Huang"> Shile Huang</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Cryptotanshinone (CPT), a fat-soluble tanshinone from Salvia miltiorrhiza Bunge, has been demonstrated to inhibit mTOR pathway, resulting in inhibition of cancer cell proliferation. However, the molecular mechanism how CPT acts on mTOR is unknown. Here, cancer cells expressing rapamycin-resistant mutant mTOR are also sensitive to CPT, while phosphorylation of AMPK and TSC2 was activated, suggesting that CPT inhibition of mTOR maybe due to activating upstream of mTOR, AMPK, but not directly binding to and inhibiting mTOR. Further results indicated that Compound C, inhibitor of AMPK, could partially reversed CPT inhibition effect on cancer cells, and dominant-negative AMPK in cancer cells conferred resistance to CPT inhibition of 4EBP1 and phosphorylation of S6K1, as well as sh-AMPK. Furthermore, compared with MEF cells with AMPK positive, MEF cells with AMPK knock out are less sensitive to CPT by the findings that 4E-BP1 and phosphorylation of S6K1 express comparatively much. Furthermore, downexpression of TSC2 slightly recovered expression of 4EBP1 and phosphorylation of S6K1, while co-immunoprecipitation of TSC2 did not affect expression of TSC1 by CPT. Collectively, the above-mentioned results suggest that CPT inhibited mTOR pathway mostly was due to activation of AMPK-TSC2 pathway rather than specific inhibition of mTOR and then induction of subsequent lethal cellular effect. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=cryptotanshinone" title="cryptotanshinone">cryptotanshinone</a>, <a href="https://publications.waset.org/abstracts/search?q=AMPK" title=" AMPK"> AMPK</a>, <a href="https://publications.waset.org/abstracts/search?q=TSC2" title=" TSC2"> TSC2</a>, <a href="https://publications.waset.org/abstracts/search?q=mTOR" title=" mTOR"> mTOR</a>, <a href="https://publications.waset.org/abstracts/search?q=cancer%20cells" title=" cancer cells"> cancer cells</a> </p> <a href="https://publications.waset.org/abstracts/2970/activation-of-ampk-tsc-axis-is-involved-in-cryptotanshinone-inhibition-of-mtor-signaling-in-cancer-cells" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/2970.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">489</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">1075</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">1074</span> Measuring the Effectiveness of Response Inhibition regarding to Motor Complexity: Evidence from the Stroop Effect</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Germ%C3%A1n%20G%C3%A1lvez-Garc%C3%ADa">Germán Gálvez-García</a>, <a href="https://publications.waset.org/abstracts/search?q=Marta%20Lavin"> Marta Lavin</a>, <a href="https://publications.waset.org/abstracts/search?q=Javiera%20Pe%C3%B1a"> Javiera Peña</a>, <a href="https://publications.waset.org/abstracts/search?q=Javier%20Albayay"> Javier Albayay</a>, <a href="https://publications.waset.org/abstracts/search?q=Claudio%20Bascour"> Claudio Bascour</a>, <a href="https://publications.waset.org/abstracts/search?q=Jesus%20Fernandez-Gomez"> Jesus Fernandez-Gomez</a>, <a href="https://publications.waset.org/abstracts/search?q=Alicia%20P%C3%A9rez-G%C3%A1lvez"> Alicia Pérez-Gálvez</a> </p> <p class="card-text"><strong>Abstract:</strong></p> We studied the effectiveness of response inhibition in movements with different degrees of motor complexity when they were executed in isolation and alternately. Sixteen participants performed the Stroop task which was used as a measure of response inhibition. Participants responded by lifting the index finger and reaching the screen with the same finger. Both actions were performed separately and alternately in different experimental blocks. Repeated measures ANOVAs were used to compare reaction time, movement time, kinematic errors and Movement errors across conditions (experimental block, movement, and congruency). Delta plots were constructed to perform distributional analyses of response inhibition and accuracy rate. The effectiveness of response inhibition did not show difference when the movements were performed in separated blocks. Nevertheless, it showed differences when they were performed alternately in the same experimental block, being more effective for the lifting action. This could be due to a competition of the available resources during a more complex scenario which also demands to adopt some strategy to avoid errors. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=response%20inhibition" title="response inhibition">response inhibition</a>, <a href="https://publications.waset.org/abstracts/search?q=motor%20complexity" title=" motor complexity"> motor complexity</a>, <a href="https://publications.waset.org/abstracts/search?q=Stroop%20task" title=" Stroop task"> Stroop task</a>, <a href="https://publications.waset.org/abstracts/search?q=delta%20plots" title=" delta plots"> delta plots</a> </p> <a href="https://publications.waset.org/abstracts/78372/measuring-the-effectiveness-of-response-inhibition-regarding-to-motor-complexity-evidence-from-the-stroop-effect" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/78372.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">394</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">1073</span> Identification of Synthetic Hybrids of 4-Thiazolidinone-Bromopyrrole Alkaloid as HIV-1 RT Inhibitors</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Rajesh%20A.%20Rane">Rajesh A. Rane</a>, <a href="https://publications.waset.org/abstracts/search?q=Shital%20S.%20Naphade"> Shital S. Naphade</a>, <a href="https://publications.waset.org/abstracts/search?q=Rajshekhar%20Karpoormath"> Rajshekhar Karpoormath</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Thiozolidin-4-one, a mimic of thiazolobenzimidazole (TBZ) has drawn many attentions due to its potent and selective inhibition against the HIV-1 and low toxicity by binding to the allosteric site of the reverse transcriptase (RT) as a non-nucleoside RT inhibitor (NNRTI). Similarly, marine bromopyrrole alkaloids are well known for their diverse array of anti-infective properties. Hence, we have reported synthesis and in vitro HIV-1 RT inhibitory activity of a series of 4-thiazolidinone-bromopyrrole alkaloid hybrids tethered with amide linker. The results of in vitro HIV-1 RT kit assay showed that some of the compounds, such as 4c, 4d, and 4i could effectively inhibit RT activity. Among them, compounds 4c having 4-chlorophenyl substituted 4-thiazolidione ring was the best one with the IC50 value of 0.26 µM. The sturdy emerges with key structure-activity relationship that pyrrole-NH-free core benefited inhibition against HIV-1 RT inhibition. This study identified conjugate 4c with potent activity and selectivity as promising compound for further drug development to HIV. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=antiviral%20drugs" title="antiviral drugs">antiviral drugs</a>, <a href="https://publications.waset.org/abstracts/search?q=bromopyrrole%20alkaloids" title=" bromopyrrole alkaloids"> bromopyrrole alkaloids</a>, <a href="https://publications.waset.org/abstracts/search?q=HIV-1%20RT%20inhibition" title=" HIV-1 RT inhibition"> HIV-1 RT inhibition</a>, <a href="https://publications.waset.org/abstracts/search?q=4-thiazolidinone" title=" 4-thiazolidinone"> 4-thiazolidinone</a> </p> <a href="https://publications.waset.org/abstracts/35304/identification-of-synthetic-hybrids-of-4-thiazolidinone-bromopyrrole-alkaloid-as-hiv-1-rt-inhibitors" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/35304.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">459</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">1072</span> Extracellular Hydrolase-Producing Bacteria Isolated from Chilca Salterns in Peru</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Carol%20N.%20Flores-Fern%C3%A1ndez">Carol N. Flores-Fernández</a>, <a href="https://publications.waset.org/abstracts/search?q=Guadalupe%20Espilco"> Guadalupe Espilco</a>, <a href="https://publications.waset.org/abstracts/search?q=Cynthia%20Esquerre"> Cynthia Esquerre</a>, <a href="https://publications.waset.org/abstracts/search?q=Amparo%20I.%20Zavaleta"> Amparo I. Zavaleta</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Saline environments represent a valuable source of enzymes with novel properties and particular features for application in food, pharmaceutical and chemical industry. This study focuses on the isolation and screening of hydrolase-producing bacteria from Chilca salterns and the evaluation of their biotechnological potential. Soil samples were collected from Chilca salterns in Peru. For the isolation, medium containing 0.2 % of yeast extract, 5 % of NaCl and 10 % of the soil sample was used. After 72 h of incubation at 37 °C, serial dilutions were made up to 10−12 dilutions, spread on agar plates with 0.5 % of yeast extract and 5 % of NaCl, and incubated at 37 °C for 48 h. Screening of hydrolase-producing bacteria was carried out for cellulases, amylases, lipases, DNase, and proteases on specific media. Moreover, protease-producing bacteria were tested using protein extracted from the following legumes as substrate: Glycine max, Lupinus mutabilis, Pisum sativum, Erythrina edulis, Cicer arietinum, Phaseolus vulgaris and Vicia faba. A total of 16 strains were isolated from soil samples. On the screening media; 75, 44, 81 and 50 % were cellulase, amylase, DNase and protease producers, respectively. Also, 19 % of the isolates produced all the hydrolytic enzymes above mentioned. Lipase producers were not found. The 37 % and 12 % of the strains grew at 20 % and 30 % of salt concentration, respectively. In addition, 75 % of the strains grew at pH range between 5 and 10. From the total of protease-producing bacteria, 100 % hydrolyzed Glycine max, Lupinus mutabilis, and Pisum sativum protein, while 87 % hydrolyzed Erythrina edulis and Cicer arietinum protein. Finally, 75 % and 50 % of the strains hydrolyzed Phaseolus vulgaris and Vicia faba protein, respectively. Hydrolase-producing bacteria isolated from Chilca salterns in Peru grew at high salt concentrations and wide range of pH. In addition, protease-producing bacteria hydrolyzed protein from different sources such as leguminous. These enzymes have great biotechnological potential and could be used for different industrial processes and applications. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=bacteria" title="bacteria">bacteria</a>, <a href="https://publications.waset.org/abstracts/search?q=extracellular" title=" extracellular"> extracellular</a>, <a href="https://publications.waset.org/abstracts/search?q=hydrolases" title=" hydrolases"> hydrolases</a>, <a href="https://publications.waset.org/abstracts/search?q=Peru" title=" Peru"> Peru</a>, <a href="https://publications.waset.org/abstracts/search?q=salterns" title=" salterns"> salterns</a> </p> <a href="https://publications.waset.org/abstracts/72791/extracellular-hydrolase-producing-bacteria-isolated-from-chilca-salterns-in-peru" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/72791.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">208</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">1071</span> Relationship Between Behavioral Inhibition/Approach System, and Perceived Stress, With White Blood Cell In Multiple Sclerosis Patients</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Amin%20Alvani">Amin Alvani</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Multiple sclerosis (MS) is a chronic, often disabling disease in which the immune system attacks the myelin sheath of neurons in the central nervous system. The present study aimed to investigate the Relationship between behavioral inhibition/approach system (BIS-BAS) and perceived stress (PS) whit control white blood cell (WBC). 60 MS patients (male=36.7, female=63.3%; age range=15-65 participated in the study and completed the demographic questionnaire, the count blood cell (CBC) test, the behavioral Activation and behavioral inhibition scale (BIS-BAS), and the perceived stress Questionnaire (PSS-14). The results revealed that Between of BAS-reward responsiveness (BAS-DR) subscale and PS, in more than MS patient (BIS), there are increase WBC. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=behavioral%20inhibition%2Fapproach%20system" title="behavioral inhibition/approach system">behavioral inhibition/approach system</a>, <a href="https://publications.waset.org/abstracts/search?q=perceived%20stress" title=" perceived stress"> perceived stress</a>, <a href="https://publications.waset.org/abstracts/search?q=white%20blood%20cell" title=" white blood cell"> white blood cell</a>, <a href="https://publications.waset.org/abstracts/search?q=multiple%20sclerosis" title=" multiple sclerosis"> multiple sclerosis</a> </p> <a href="https://publications.waset.org/abstracts/165572/relationship-between-behavioral-inhibitionapproach-system-and-perceived-stress-with-white-blood-cell-in-multiple-sclerosis-patients" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/165572.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">91</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">1070</span> Synthesis, Electrochemical and Theoretical Study of Corrosion Inhibition on Carbon Steel in 1M HCl Medium by 2,2'-(piperazine-1,4-diyl)bis(N-(4-bromophenyl)acetamide)</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Tanghourte%20Mohamed">Tanghourte Mohamed</a>, <a href="https://publications.waset.org/abstracts/search?q=Ouassou%20Nazih"> Ouassou Nazih</a>, <a href="https://publications.waset.org/abstracts/search?q=El%20Mesky%20Mohammed"> El Mesky Mohammed</a>, <a href="https://publications.waset.org/abstracts/search?q=Znini%20Mohamed"> Znini Mohamed</a>, <a href="https://publications.waset.org/abstracts/search?q=Mabrouk%20El%20Houssine"> Mabrouk El Houssine</a> </p> <p class="card-text"><strong>Abstract:</strong></p> In the present study, a distinct organic inhibitor, namely 2,2'-(piperazine-1,4-diyl)bis(N-(4-bromophenyl)acetamide) (PBRA), was synthesized and characterized using ¹H, ¹³C NMR, and IR spectroscopy. Subsequently, the inhibition effect of PBRA on the corrosion of carbon steel in 1 M HCl was studied using electrochemical measurements such as potentiodynamic polarization (PDP) and electrochemical impedance spectroscopy (EIS). The results showed that the inhibition efficiency increased with concentration, reaching 87% at 10-³M. Furthermore, PBRA remained effective at temperatures ranging from 298 to 328 K. The adsorption of the inhibitor onto carbon steel was well described by the Langmuir adsorption isotherm. Additionally, a correlation between the molecular structure and quantum chemistry indices was established using density functional theory (DFT). <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=synthesis" title="synthesis">synthesis</a>, <a href="https://publications.waset.org/abstracts/search?q=corrosion" title=" corrosion"> corrosion</a>, <a href="https://publications.waset.org/abstracts/search?q=inhibition" title=" inhibition"> inhibition</a>, <a href="https://publications.waset.org/abstracts/search?q=piperazine" title=" piperazine"> piperazine</a>, <a href="https://publications.waset.org/abstracts/search?q=efficacy" title=" efficacy"> efficacy</a>, <a href="https://publications.waset.org/abstracts/search?q=isotherm" title=" isotherm"> isotherm</a>, <a href="https://publications.waset.org/abstracts/search?q=acetamide" title=" acetamide"> acetamide</a> </p> <a href="https://publications.waset.org/abstracts/194779/synthesis-electrochemical-and-theoretical-study-of-corrosion-inhibition-on-carbon-steel-in-1m-hcl-medium-by-22-piperazine-14-diylbisn-4-bromophenylacetamide" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/194779.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">5</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">1069</span> Allura Red, Sunset Yellow and Amaranth Azo Dyes for Corrosion Inhibition of Mild Steel in 0.5 H₂SO₄ Solutions</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Ashish%20Kumar%20Singh">Ashish Kumar Singh</a>, <a href="https://publications.waset.org/abstracts/search?q=Preeti%20Tiwari"> Preeti Tiwari</a>, <a href="https://publications.waset.org/abstracts/search?q=Shubham%20Srivastava"> Shubham Srivastava</a>, <a href="https://publications.waset.org/abstracts/search?q=Rajiv%20Prakash"> Rajiv Prakash</a>, <a href="https://publications.waset.org/abstracts/search?q=Herman%20Terryn"> Herman Terryn</a>, <a href="https://publications.waset.org/abstracts/search?q=Gopal%20Ji"> Gopal Ji</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Corrosion inhibition potential of azo dyes namely Allura red (AR), Sunset Yellow (SY) and Amaranth (AN) have been investigated in 0.5 M H2SO4 solutions by electrochemical impedance spectroscopy (EIS), Tafel polarization curves, linear polarization curves, open circuit potential (ocp) curves, UV-Visible spectroscopy, Fourier Transform Infrared spectroscopy (FTIR) and scanning electron microscopy (SEM) techniques. Amaranth dye is found to provide highest corrosion inhibition (90 %) against mild steel corrosion in sulfuric acid solutions among all the tested dyes; while SY and AR dye shows 80% and 78% corrosion inhibition efficiency respectively. The electrochemical measurements and surface morphology analysis reveal that molecular adsorption of dyes at metal acid interface is accountable for inhibition of mild steel corrosion in H2SO4 solutions. The adsorption behavior of dyes has been investigated by various isotherms models, which verifies that it is in accordance with Langmuir isotherm. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=mild%20steel" title="mild steel">mild steel</a>, <a href="https://publications.waset.org/abstracts/search?q=Azo%20dye" title=" Azo dye"> Azo dye</a>, <a href="https://publications.waset.org/abstracts/search?q=EIS" title=" EIS"> EIS</a>, <a href="https://publications.waset.org/abstracts/search?q=Langmuir%20isotherm" title=" Langmuir isotherm"> Langmuir isotherm</a> </p> <a href="https://publications.waset.org/abstracts/55946/allura-red-sunset-yellow-and-amaranth-azo-dyes-for-corrosion-inhibition-of-mild-steel-in-05-h2so4-solutions" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/55946.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">375</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">1068</span> The Effect of Artesunate on Myeloperoxidase Activity of Human Polymorphonuclear Neutrophil</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=J.%20B.%20Minari">J. B. Minari</a>, <a href="https://publications.waset.org/abstracts/search?q=O.%20B.%20Oloyede"> O. B. Oloyede</a>, <a href="https://publications.waset.org/abstracts/search?q=A.%20A.%20Odutuga"> A. A. Odutuga</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Myeloperoxidase is the most abundant enzyme found in the polymorphonuclear neutrophil and is known to play a central role in the host defense system of the leukocyte. The enzyme has been reported to interact with some drugs to generate free radical which inhibits its activity. This study investigated the effects of artesunate on the activity of the enzyme and the subsequent effect on the host immune system. In investigating the effects of the drugs on myeloperoxidase, the influence of concentration, pH, partition ratio estimation and kinetics of inhibition were studied. This study showed that artesunate is concentration-dependent inhibitor of myeloperoxidase with an IC50 of 0.078mM. Partition ratio estimation showed that 60 enzymatic turnover cycles are required for complete inhibition of myeloperoxidase in the presence of artesunate. The influence of pH on the effect of artesunate on the enzyme showed least activity of myeloperoxidase at physiological pH. The kinetic inhibition studies showed that artesunate caused a competitive inhibition with an increase in the Km value from 0.12mM to 0.26mM and no effect on the Vmax value. The Ki value was estimated to be 2.5mM. The results obtained from this study show that artesunate is a potent inhibitor of myeloperoxidase and it is capable of inactivating the enzyme. It is considered that the inhibition of myeloperoxidase in the presence of artesunate as revealed in this study may partly explain the impairment of polymorphonuclear neutrophil and consequent reduction of the strength of the host defense system against secondary infections. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=myeloperoxidase" title="myeloperoxidase">myeloperoxidase</a>, <a href="https://publications.waset.org/abstracts/search?q=artesunate" title=" artesunate"> artesunate</a>, <a href="https://publications.waset.org/abstracts/search?q=inhibition" title=" inhibition"> inhibition</a>, <a href="https://publications.waset.org/abstracts/search?q=nuetrophill" title=" nuetrophill "> nuetrophill </a> </p> <a href="https://publications.waset.org/abstracts/17692/the-effect-of-artesunate-on-myeloperoxidase-activity-of-human-polymorphonuclear-neutrophil" class="btn btn-primary btn-sm">Procedia</a> <a 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