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proteins</title> <meta name="description" content="Search results for: fluorescent proteins"> <meta name="keywords" content="fluorescent proteins"> <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="fluorescent proteins"> <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> 1274</div> </div> </div> </div> <h1 class="mt-3 mb-3 text-center" style="font-size:1.6rem;">Search results for: fluorescent proteins</h1> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">1274</span> The Response of Adaptive Mechanism of Fluorescent Proteins from Coral Species and Target Cell Properties on Signalling Capacity as Biosensor</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Elif%20Tugce%20Aksun%20Tumerkan">Elif Tugce Aksun Tumerkan</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Fluorescent proteins (FPs) have become very popular since green fluorescent protein discovered from crystal jellyfish. It is known that Anthozoa species have a wide range of chromophore organisms, and the initial crystal structure for non-fluorescent chromophores obtained from the reef-building coral has been determined. There are also differently coloured pigments in non-bioluminescent Anthozoa zooxanthellate and azooxanthellate which are frequently members of the GFP-like protein family. The development of fluorescent proteins (FPs) and their applications is an outstanding example of basic science leading to practical biotechnological and medical applications. Fluorescent proteins have several applications in science and are used as important indicators in molecular biology and cell-based research. With rising interest in cell biology, FPs have used as biosensor indicators and probes in pharmacology and cell biology. Using fluorescent proteins in genetically encoded metabolite sensors has many advantages than chemical probes for metabolites such as easily introduced into any cell or organism in any sub-cellular localization and giving chance to fixing to fluoresce of different colours or characteristics. There are different factors effects to signalling mechanism when they used as a biosensor. While there are wide ranges of research have been done on the significance and applications of fluorescent proteins, the cell signalling response of FPs and target cell are less well understood. In this study, it was aimed to clarify the response of adaptive mechanisms of coral species such as pH, temperature and symbiotic relationship and target cells properties on the signalling capacity. Corals are a rich natural source of fluorescent proteins that change with environmental conditions such as light, heat stress and injury. Adaptation mechanism of coral species to these types of environmental variations is important factor due to FPs properties have affected by this mechanism. Since fluorescent proteins obtained from nature, their own ecological property like the symbiotic relationship is observed very commonly in coral species and living conditions have the impact on FPs efficiency. Target cell properties also have an effect on signalling and visualization. The dynamicity of detector that used for reading fluorescence and the level of background fluorescence are key parameters for the quality of the fluorescent signal. Among the factors, it can be concluded that coral species adaptive characteristics have the strongest effect on FPs signalling capacity. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=biosensor" title="biosensor">biosensor</a>, <a href="https://publications.waset.org/abstracts/search?q=cell%20biology" title=" cell biology"> cell biology</a>, <a href="https://publications.waset.org/abstracts/search?q=environmental%20conditions" title=" environmental conditions"> environmental conditions</a>, <a href="https://publications.waset.org/abstracts/search?q=fluorescent%20protein" title=" fluorescent protein"> fluorescent protein</a>, <a href="https://publications.waset.org/abstracts/search?q=sea%20anemone" title=" sea anemone"> sea anemone</a> </p> <a href="https://publications.waset.org/abstracts/94010/the-response-of-adaptive-mechanism-of-fluorescent-proteins-from-coral-species-and-target-cell-properties-on-signalling-capacity-as-biosensor" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/94010.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">170</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">1273</span> Gene Expression and Staining Agents: Exploring the Factors That Influence the Electrophoretic Properties of Fluorescent Proteins</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Elif%20Tugce%20Aksun%20Tumerkan">Elif Tugce Aksun Tumerkan</a>, <a href="https://publications.waset.org/abstracts/search?q=Chris%20Lowe"> Chris Lowe</a>, <a href="https://publications.waset.org/abstracts/search?q=Hannah%20Krupa"> Hannah Krupa</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Fluorescent proteins are self-sufficient in forming chromophores with a visible wavelength from 3 amino acids sequence within their own polypeptide structure. This chromophore – a molecule that absorbs a photon of light and exhibits an energy transition equal to the energy of the absorbed photon. Fluorescent proteins (FPs) consisted of a chain of 238 amino acid residues and composed of 11 beta strands shaped in a cylinder surrounding an alpha helix structure. A better understanding of the system of the chromospheres and the increasing advance in protein engineering in recent years, the properties of FPs offers the potential for new applications. They have used sensors and probes in molecular biology and cell-based research that giving a chance to observe these FPs tagged cell localization, structural variation and movement. For clarifying functional uses of fluorescent proteins, electrophoretic properties of these proteins are one of the most important parameters. Sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) analysis is used for determining electrophoretic properties commonly. While there are many techniques are used for determining the functionality of protein-based research, SDS-PAGE analysis can only provide a molecular level assessment of the proteolytic fragments. Before SDS-PAGE analysis, fluorescent proteins need to successfully purified. Due to directly purification of the target, FPs is difficult from the animal, gene expression is commonly used which must be done by transformation with the plasmid. Furthermore, used gel within electrophoresis and staining agents properties have a key role. In this review, the different factors that have the impact on the electrophoretic properties of fluorescent proteins explored. Fluorescent protein separation and purification are the essential steps before electrophoresis that should be done very carefully. For protein purification, gene expression process and following steps have a significant function. For successful gene expression, the properties of selected bacteria for expression, used plasmid are essential. Each bacteria has own characteristics which are very sensitive to gene expression, also used procedure is the important factor for fluorescent protein expression. Another important factors are gel formula and used staining agents. Gel formula has an effect on the specific proteins mobilization and staining with correct agents is a key step for visualization of electrophoretic bands of protein. Visuality of proteins can be changed depending on staining reagents. Apparently, this review has emphasized that gene expression and purification have a stronger effect than electrophoresis protocol and staining agents. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=cell%20biology" title="cell biology">cell biology</a>, <a href="https://publications.waset.org/abstracts/search?q=gene%20expression" title=" gene expression"> gene expression</a>, <a href="https://publications.waset.org/abstracts/search?q=staining%20agents" title=" staining agents"> staining agents</a>, <a href="https://publications.waset.org/abstracts/search?q=SDS-page" title=" SDS-page"> SDS-page</a> </p> <a href="https://publications.waset.org/abstracts/94082/gene-expression-and-staining-agents-exploring-the-factors-that-influence-the-electrophoretic-properties-of-fluorescent-proteins" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/94082.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">194</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">1272</span> Selection of Green Fluorescent Protein and mCherry Nanobodies Using the Yeast Surface Display Method</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Lavinia%20Ruta">Lavinia Ruta</a>, <a href="https://publications.waset.org/abstracts/search?q=Ileana%20Farcasanu"> Ileana Farcasanu</a> </p> <p class="card-text"><strong>Abstract:</strong></p> The yeast surface display (YSD) technique enables the expression of proteins on yeast cell surfaces, facilitating the identification and isolation of proteins with targeted binding properties, such as nanobodies. Nanobodies, derived from camelid species, are single-domain antibody fragments renowned for their high affinity and specificity towards target proteins, making them valuable in research and potentially in therapeutics. Their advantages include a compact size (~15 kDa), robust stability, and the ability to target challenging epitopes. The project endeavors to establish and validate a platform for producing Green Fluorescent Protein (GFP) and mCherry nanobodies using the yeast surface display method. mCherry, a prevalent red fluorescent protein sourced from coral species, is commonly utilized as a genetic marker in biological studies due to its vibrant red fluorescence. The GFP-nanobody, a single variable domain of heavy-chain antibodies (VHH), exhibits specific binding to GFP, offering a potent means for isolating and engineering fluorescent protein fusions across various biological research domains. Both GFP and mCherry nanobodies find specific utility in cellular imaging and protein analysis applications. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=YSD" title="YSD">YSD</a>, <a href="https://publications.waset.org/abstracts/search?q=nanobodies" title=" nanobodies"> nanobodies</a>, <a href="https://publications.waset.org/abstracts/search?q=GFP" title=" GFP"> GFP</a>, <a href="https://publications.waset.org/abstracts/search?q=Saccharomyces%20cerevisiae" title=" Saccharomyces cerevisiae"> Saccharomyces cerevisiae</a> </p> <a href="https://publications.waset.org/abstracts/184472/selection-of-green-fluorescent-protein-and-mcherry-nanobodies-using-the-yeast-surface-display-method" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/184472.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">61</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">1271</span> Crystallography Trials of Escherichia coli Nitrate Transporter, NarU</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Naureen%20Akhtar">Naureen Akhtar</a> </p> <p class="card-text"><strong>Abstract:</strong></p> The stability of the protein in detergent-containing solution is the key for its successful crystallisation. Fluorescence-detection size-exclusion chromatography (FSEC) is a potential approach for screening monodispersity as well as the stability of protein in a detergent-containing-solution. In this present study, covalently linked Green Fluorescent Protein (GFP) to bacterial nitrate transporter, NarU from Escherichia coli was studied for pre-crystallisation trials by FSEC. Immobilised metal ion affinity chromatography (IMAC) and gel filtration were employed for their purification. The main objectives of this study were over-expression, detergent screening and crystallisation of nitrate transporter proteins. This study could not produce enough proteins that could realistically be taken forward to achieve the objectives set for this particular research. In future work, different combinations of variables like vectors, tags, creation of mutant proteins, host cells, position of GFP (N- or C-terminal) and/or membrane proteins would be tried to determine the best combination as the principle of technique is still promising. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=transporters" title="transporters">transporters</a>, <a href="https://publications.waset.org/abstracts/search?q=detergents" title=" detergents"> detergents</a>, <a href="https://publications.waset.org/abstracts/search?q=over-expression" title=" over-expression"> over-expression</a>, <a href="https://publications.waset.org/abstracts/search?q=crystallography" title=" crystallography"> crystallography</a> </p> <a href="https://publications.waset.org/abstracts/15732/crystallography-trials-of-escherichia-coli-nitrate-transporter-naru" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/15732.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">477</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">1270</span> In vitro Protein Folding and Stability Using Thermostable Exoshells </h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Siddharth%20Deshpande">Siddharth Deshpande</a>, <a href="https://publications.waset.org/abstracts/search?q=Nihar%20Masurkar"> Nihar Masurkar</a>, <a href="https://publications.waset.org/abstracts/search?q=Vallerinteavide%20Mavelli%20Girish"> Vallerinteavide Mavelli Girish</a>, <a href="https://publications.waset.org/abstracts/search?q=Malan%20Desai"> Malan Desai</a>, <a href="https://publications.waset.org/abstracts/search?q=Chester%20Drum"> Chester Drum</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Folding and stabilization of recombinant proteins remain a consistent challenge for industrial and therapeutic applications. Proteins derived from thermophilic bacteria often have superior expression and stability qualities. To develop a generalizable approach to protein folding and stabilization, we tested the hypothesis that wrapping a thermostable exoshell around a protein substrate would aid folding and impart thermostable qualities to the internalized substrate. To test the effect of internalizing a protein within a thermostable exoshell (tES), we tested in vitro folding and stability using green fluorescent protein (GFPuv), horseradish peroxidase (HRP) and renilla luciferase (rLuc). The 8nm interior volume of a thermostable ferritin assembly was engineered to accommodate foreign proteins and either present a positive, neutral or negative interior charge environment. We further engineered the tES complex to reversibly assemble and disassemble with pH titration. Template proteins were expressed as inclusion bodies and an in vitro folding protocol was developed that forced proteins to fold inside a single tES. Functional yield was improved 100-fold, 100-fold and 150-fold with use of tES for GFPuv, HRP and rLuc respectively and was highly dependent on the internal charge environment of the tES. After folding, functional proteins could be released from the tES folding cavity using size exclusion chromatography at pH 5.8. Internalized proteins were tested for improved stability against thermal, organic, urea and guanidine denaturation. Our results demonstrated that thermostable exoshells can efficiently refold and stabilize inactive aggregates into functional proteins. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=thermostable%20shell" title="thermostable shell">thermostable shell</a>, <a href="https://publications.waset.org/abstracts/search?q=in%20vitro%20folding" title=" in vitro folding"> in vitro folding</a>, <a href="https://publications.waset.org/abstracts/search?q=stability" title=" stability"> stability</a>, <a href="https://publications.waset.org/abstracts/search?q=functional%20yield" title=" functional yield"> functional yield</a> </p> <a href="https://publications.waset.org/abstracts/72637/in-vitro-protein-folding-and-stability-using-thermostable-exoshells" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/72637.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">249</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">1269</span> Reflector Arrangement Effect on Ultraviolet Lamp Performance by CFX Simulation</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=William%20Sidharta">William Sidharta</a>, <a href="https://publications.waset.org/abstracts/search?q=Chin-Tu%20Lu"> Chin-Tu Lu</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Fluorescent ultraviolet lamp generates ultraviolet light which is commonly used in industrial field with certain purposes especially for curing process. Due to the value of inefficiency, there are changes in energy from electrical energy to the heat energy and this would make a defect on the industrial product caused by high temperature of lamp tube during ultraviolet light emission. The condition of industrial scale is further worsening, since commonly using dozens of fluorescent ultraviolet lamps to support huge production process and then it will generates much more heat energy. The maximum temperature of fluorescent ultraviolet lamp will get affected by arranging the lamp tube reflector and this study presents CFX simulation results of the maximum lamp tube temperature with some different reflector arrangements on purely natural convection phenomena. There exists certain spaces value of the reflector and the lamp tube to obtaining lower maximum temperature of the fluorescent ultraviolet lamp. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=CFX%20simulation" title="CFX simulation">CFX simulation</a>, <a href="https://publications.waset.org/abstracts/search?q=fluorescent%20UV%20lamp" title=" fluorescent UV lamp"> fluorescent UV lamp</a>, <a href="https://publications.waset.org/abstracts/search?q=lamp%20tube%20reflector" title=" lamp tube reflector"> lamp tube reflector</a>, <a href="https://publications.waset.org/abstracts/search?q=UV%20light" title=" UV light "> UV light </a> </p> <a href="https://publications.waset.org/abstracts/25442/reflector-arrangement-effect-on-ultraviolet-lamp-performance-by-cfx-simulation" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/25442.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">465</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">1268</span> Using Artificial Neural Networks for Optical Imaging of Fluorescent Biomarkers </h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=K.%20A.%20Laptinskiy">K. A. Laptinskiy</a>, <a href="https://publications.waset.org/abstracts/search?q=S.%20A.%20Burikov"> S. A. Burikov</a>, <a href="https://publications.waset.org/abstracts/search?q=A.%20M.%20Vervald"> A. M. Vervald</a>, <a href="https://publications.waset.org/abstracts/search?q=S.%20A.%20Dolenko"> S. A. Dolenko</a>, <a href="https://publications.waset.org/abstracts/search?q=T.%20A.%20Dolenko"> T. A. Dolenko</a> </p> <p class="card-text"><strong>Abstract:</strong></p> The article presents the results of the application of artificial neural networks to separate the fluorescent contribution of nanodiamonds used as biomarkers, adsorbents and carriers of drugs in biomedicine, from a fluorescent background of own biological fluorophores. The principal possibility of solving this problem is shown. Use of neural network architecture let to detect fluorescence of nanodiamonds against the background autofluorescence of egg white with high accuracy - better than 3 ug/ml. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=artificial%20neural%20networks" title="artificial neural networks">artificial neural networks</a>, <a href="https://publications.waset.org/abstracts/search?q=fluorescence" title=" fluorescence"> fluorescence</a>, <a href="https://publications.waset.org/abstracts/search?q=data%20aggregation" title=" data aggregation"> data aggregation</a>, <a href="https://publications.waset.org/abstracts/search?q=biomarkers" title=" biomarkers"> biomarkers</a> </p> <a href="https://publications.waset.org/abstracts/14494/using-artificial-neural-networks-for-optical-imaging-of-fluorescent-biomarkers" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/14494.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">710</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">1267</span> Albumin-Induced Turn-on Fluorescence in Molecular Engineered Fluorescent Probe for Biomedical Application</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Raja%20Chinnappan">Raja Chinnappan</a>, <a href="https://publications.waset.org/abstracts/search?q=Huda%20Alanazi"> Huda Alanazi</a>, <a href="https://publications.waset.org/abstracts/search?q=Shanmugam%20Easwaramoorthi"> Shanmugam Easwaramoorthi</a>, <a href="https://publications.waset.org/abstracts/search?q=Tanveer%20Mir"> Tanveer Mir</a>, <a href="https://publications.waset.org/abstracts/search?q=Balamurugan%20Kanagasabai"> Balamurugan Kanagasabai</a>, <a href="https://publications.waset.org/abstracts/search?q=Ahmed%20Yaqinuddin"> Ahmed Yaqinuddin</a>, <a href="https://publications.waset.org/abstracts/search?q=Sandhanasamy%20Devanesan"> Sandhanasamy Devanesan</a>, <a href="https://publications.waset.org/abstracts/search?q=Mohamad%20S.%20AlSalhi"> Mohamad S. AlSalhi</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Serum albumin (SA) is a highly rich water-soluble protein in plasma. It is known to maintain the living organisms' health and help to maintain the proper liver function, kidney function, and plasma osmolality in the body. Low levels of serum albumin are an indication of liver failure and chronic hepatitis. Therefore, it is important to have a low-cost, accurate and rapid method. In this study, we designed a fluorescent probe, triphenylamine rhodanine-3-acetic acid (mRA), which triggers the fluorescence signal upon binding with serum albumin (SA). mRA is a bifunctional molecule with twisted intramolecular charge transfer (TICT)-induced emission characteristics. An aqueous solution of mRA has an insignificant fluorescence signal; however, when mRA binds to SA, it undergoes TICT and turns on the fluorescence emission. A SA dose-dependent fluorescence signal was performed, and the limit of detection was found to be less than ng/mL. The specific binding of SA was tested from the cross-reactivity study using similar structural or functional proteins. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=serum%20albumin" title="serum albumin">serum albumin</a>, <a href="https://publications.waset.org/abstracts/search?q=fluorescent%20sensing%20probe" title=" fluorescent sensing probe"> fluorescent sensing probe</a>, <a href="https://publications.waset.org/abstracts/search?q=liver%20diseases" title=" liver diseases"> liver diseases</a>, <a href="https://publications.waset.org/abstracts/search?q=twisted%20intramolecular%20charge%20transfer" title=" twisted intramolecular charge transfer"> twisted intramolecular charge transfer</a> </p> <a href="https://publications.waset.org/abstracts/193364/albumin-induced-turn-on-fluorescence-in-molecular-engineered-fluorescent-probe-for-biomedical-application" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/193364.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">18</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">1266</span> Green Synthesis of Red-Fluorescent Gold Nanoclusters: Characterization and Application for Breast Cancer Detection</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Agn%C4%97%20Mikalauskait%C4%97">Agnė Mikalauskaitė</a>, <a href="https://publications.waset.org/abstracts/search?q=Renata%20Karpicz"> Renata Karpicz</a>, <a href="https://publications.waset.org/abstracts/search?q=Vitalijus%20Karabanovas"> Vitalijus Karabanovas</a>, <a href="https://publications.waset.org/abstracts/search?q=Ar%C5%ABnas%20Jagminas"> Arūnas Jagminas</a> </p> <p class="card-text"><strong>Abstract:</strong></p> The use of biocompatible precursors for the synthesis and stabilization of fluorescent gold nanoclusters (NCs) with strong red photoluminescence creates an important link between natural sciences and nanotechnology. Herein, we report the cost-effective synthesis of Au nanoclusters by templating and reduction of chloroauric acid with the cheap amino acid food supplements. This synthesis under the optimized conditions leads to the formation of biocompatible Au NCs having good stability and intense red photoluminescence, peaked at 680 to 705 nm, with a quantum yield (QY) of ≈7% and the average lifetime of up to several µs. The composition and luminescent properties of the obtained NCs were compared with ones formed via well-known bovine serum albumin reduction approach. Our findings implied that synthesized Au NCs tend to accumulate in more tumorigenic breast cancer cells (line MDA-MB-213) and after dialysis can be prospective for bio imagining. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=gold%20nanoclusters" title="gold nanoclusters">gold nanoclusters</a>, <a href="https://publications.waset.org/abstracts/search?q=proteins" title=" proteins"> proteins</a>, <a href="https://publications.waset.org/abstracts/search?q=materials%20chemistry" title=" materials chemistry"> materials chemistry</a>, <a href="https://publications.waset.org/abstracts/search?q=red-photoluminescence" title=" red-photoluminescence"> red-photoluminescence</a>, <a href="https://publications.waset.org/abstracts/search?q=bioimaging" title=" bioimaging"> bioimaging</a> </p> <a href="https://publications.waset.org/abstracts/62262/green-synthesis-of-red-fluorescent-gold-nanoclusters-characterization-and-application-for-breast-cancer-detection" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/62262.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">278</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">1265</span> Detection of Latent Fingerprints Recovered from Arson Simulation by a Novel Fluorescent Method</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Somayeh%20Khanjani">Somayeh Khanjani</a>, <a href="https://publications.waset.org/abstracts/search?q=Samaneh%20Nabavi"> Samaneh Nabavi</a>, <a href="https://publications.waset.org/abstracts/search?q=Shirin%20Jalili"> Shirin Jalili</a>, <a href="https://publications.waset.org/abstracts/search?q=Afshin%20Khara"> Afshin Khara</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Fingerprints are area source of ubiquitous evidence and consequential for establishing identity. The detection and subsequent development of fingerprints are thus inevitable in criminal investigations. This becomes a difficult task in the case of certain extreme conditions like fire. A fire scene may be accidental or arson. The evidence subjected to fire is generally overlooked as there is a misconception that they are damaged. There are several scientific approaches to determine whether the fire was deliberate or not. In such as scenario, fingerprints may be most critical to link the perpetrator to the crime. The reason for this may be the destructive nature of fire. Fingerprints subjected to fire are exposed to high temperatures, soot deposition, electromagnetic radiation, and subsequent water force. It is believed that these phenomena damage the fingerprint. A novel fluorescent and a pre existing small particle reagent were investigated for the same. Zinc carbonates based fluorescent small particle reagent was capable of developing latent fingerprints exposed to a maximum temperature of 800 ̊C. Fluorescent SPR may prove very useful in such cases. Fluorescent SPR reagent based on zinc carbonate is a potential method for developing fingerprints from arson sites. The method is cost effective and non hazardous. This formulation is suitable for developing fingerprints exposed to fire/ arson. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=fingerprint" title="fingerprint">fingerprint</a>, <a href="https://publications.waset.org/abstracts/search?q=small%20particle%20reagent%20%28SPR%29" title=" small particle reagent (SPR)"> small particle reagent (SPR)</a>, <a href="https://publications.waset.org/abstracts/search?q=arson" title=" arson"> arson</a>, <a href="https://publications.waset.org/abstracts/search?q=novel%20fluorescent" title=" novel fluorescent "> novel fluorescent </a> </p> <a href="https://publications.waset.org/abstracts/28086/detection-of-latent-fingerprints-recovered-from-arson-simulation-by-a-novel-fluorescent-method" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/28086.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">472</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">1264</span> Computational Screening of Secretory Proteins with Brain-Specific Expression in Glioblastoma Multiforme</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Sumera">Sumera</a>, <a href="https://publications.waset.org/abstracts/search?q=Sanila%20Amber"> Sanila Amber</a>, <a href="https://publications.waset.org/abstracts/search?q=Fatima%20Javed%20Mirza"> Fatima Javed Mirza</a>, <a href="https://publications.waset.org/abstracts/search?q=Amjad%20Ali"> Amjad Ali</a>, <a href="https://publications.waset.org/abstracts/search?q=Saadia%20Zahid"> Saadia Zahid</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Glioblastoma multiforme (GBM) is a widely spread and fatal primary brain tumor with an increased risk of relapse in spite of aggressive treatment. The current procedures for GBM diagnosis include invasive procedures i.e. resection or biopsy, to acquire tumor mass. Implementation of negligibly invasive tests as a potential diagnostic technique and biofluid-based monitoring of GBM stresses on discovering biomarkers in CSF and blood. Therefore, we performed a comprehensive in silico analysis to identify potential circulating biomarkers for GBM. Initially, six gene and protein databases were utilized to mine brain-specific proteins. The resulting proteins were filtered using a channel of five tools to predict the secretory proteins. Subsequently, the expression profile of the secreted proteins was verified in the brain and blood using two databases. Additional verification of the resulting proteins was done using Plasma Proteome Database (PPD) to confirm their presence in blood. The final set of proteins was searched in literature for their relationship with GBM, keeping a special emphasis on secretome proteome. 2145 proteins were firstly mined as brain-specific, out of which 69 proteins were identified as secretory in nature. Verification of expression profile in brain and blood eliminated 58 proteins from the 69 proteins, providing a final list of 11 proteins. Further verification of these 11 proteins further eliminated 2 proteins, giving a final set of nine secretory proteins i.e. OPCML, NPTX1, LGI1, CNTN2, LY6H, SLIT1, CREG2, GDF1 and SERPINI1. Out of these 9 proteins, 7 were found to be linked to GBM, whereas 2 proteins are not investigated in GBM so far. We propose that these secretory proteins can serve as potential circulating biomarker signatures of GBM and will facilitate the development of minimally invasive diagnostic methods and novel therapeutic interventions for GBM. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=glioblastoma%20multiforme" title="glioblastoma multiforme">glioblastoma multiforme</a>, <a href="https://publications.waset.org/abstracts/search?q=secretory%20proteins" title=" secretory proteins"> secretory proteins</a>, <a href="https://publications.waset.org/abstracts/search?q=brain%20secretome" title=" brain secretome"> brain secretome</a>, <a href="https://publications.waset.org/abstracts/search?q=biomarkers" title=" biomarkers"> biomarkers</a> </p> <a href="https://publications.waset.org/abstracts/144723/computational-screening-of-secretory-proteins-with-brain-specific-expression-in-glioblastoma-multiforme" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/144723.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">152</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">1263</span> Plasma Properties Effect on Fluorescent Tube Plasma Antenna Performance</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=A.%20N.%20Dagang">A. N. Dagang</a>, <a href="https://publications.waset.org/abstracts/search?q=E.%20I.%20Ismail"> E. I. Ismail</a>, <a href="https://publications.waset.org/abstracts/search?q=Z.%20Zakaria"> Z. Zakaria</a> </p> <p class="card-text"><strong>Abstract:</strong></p> This paper presents the analysis on the performance of monopole antenna with fluorescent tubes. In this research, the simulation and experimental approach is conducted. The fluorescent tube with different length and size is designed using Computer Simulation Technology (CST) software and the characteristics of antenna parameter are simulated throughout the software. CST was used to simulate antenna parameters such as return loss, resonant frequency, gain and directivity. Vector Network Analyzer (VNA) was used to measure the return loss of plasma antenna in order to validate the simulation results. In the simulation and experiment, the supply frequency is set starting from 1 GHz to 10 GHz. The results show that the return loss of plasma antenna changes when size of fluorescent tubes is varied, correspond to the different plasma properties. It shows that different values of plasma properties such as plasma frequency and collision frequency gives difference result of return loss, gain and directivity. For the gain, the values range from 2.14 dB to 2.36 dB. The return loss of plasma antenna offers higher value range from -22.187 dB to -32.903 dB. The higher the values of plasma frequency and collision frequency, the higher return loss can be obtained. The values obtained are comparative to the conventional type of metal antenna. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=plasma%20antenna" title="plasma antenna">plasma antenna</a>, <a href="https://publications.waset.org/abstracts/search?q=fluorescent%20tube" title=" fluorescent tube"> fluorescent tube</a>, <a href="https://publications.waset.org/abstracts/search?q=CST" title=" CST"> CST</a>, <a href="https://publications.waset.org/abstracts/search?q=plasma%20parameters" title=" plasma parameters"> plasma parameters</a> </p> <a href="https://publications.waset.org/abstracts/52421/plasma-properties-effect-on-fluorescent-tube-plasma-antenna-performance" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/52421.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">1262</span> Advanced Real-Time Fluorescence Imaging System for Rat's Femoral Vein Thrombosis Monitoring</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Sang%20Hun%20Park">Sang Hun Park</a>, <a href="https://publications.waset.org/abstracts/search?q=Chul%20Gyu%20Song"> Chul Gyu Song</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Artery and vein occlusion changes observed in patients and experimental animals are unexplainable symptoms. As the fat accumulated in cardiovascular ruptures, it causes vascular blocking. Likewise, early detection of cardiovascular disease can be useful for treatment. In this study, we used the mouse femoral occlusion model to observe the arterial and venous occlusion changes without darkroom. We observed the femoral arterial flow pattern changes by proposed fluorescent imaging system using an animal model of thrombosis. We adjusted the near-infrared light source current in order to control the intensity of the fluorescent substance light. We got the clear fluorescent images and femoral artery flow pattern were measured by a 5-minute interval. The result showed that the fluorescent substance flowing in the femoral arteries were accumulated in thrombus as time passed, and the fluorescence of other vessels gradually decreased. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=thrombus" title="thrombus">thrombus</a>, <a href="https://publications.waset.org/abstracts/search?q=fluorescence" title=" fluorescence"> fluorescence</a>, <a href="https://publications.waset.org/abstracts/search?q=femoral" title=" femoral"> femoral</a>, <a href="https://publications.waset.org/abstracts/search?q=arteries" title=" arteries"> arteries</a> </p> <a href="https://publications.waset.org/abstracts/40585/advanced-real-time-fluorescence-imaging-system-for-rats-femoral-vein-thrombosis-monitoring" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/40585.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">344</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">1261</span> Computing the Similarity and the Diversity in the Species Based on Cronobacter Genome</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=E.%20Al%20Daoud">E. Al Daoud</a> </p> <p class="card-text"><strong>Abstract:</strong></p> The purpose of computing the similarity and the diversity in the species is to trace the process of evolution and to find the relationship between the species and discover the unique, the special, the common and the universal proteins. The proteins of the whole genome of 40 species are compared with the cronobacter genome which is used as reference genome. More than 3 billion pairwise alignments are performed using blastp. Several findings are introduced in this study, for example, we found 172 proteins in cronobacter genome which have insignificant hits in other species, 116 significant proteins in the all tested species with very high score value and 129 common proteins in the plants but have insignificant hits in mammals, birds, fishes, and insects. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=genome" title="genome">genome</a>, <a href="https://publications.waset.org/abstracts/search?q=species" title=" species"> species</a>, <a href="https://publications.waset.org/abstracts/search?q=blastp" title=" blastp"> blastp</a>, <a href="https://publications.waset.org/abstracts/search?q=conserved%20genes" title=" conserved genes"> conserved genes</a>, <a href="https://publications.waset.org/abstracts/search?q=Cronobacter" title=" Cronobacter"> Cronobacter</a> </p> <a href="https://publications.waset.org/abstracts/82396/computing-the-similarity-and-the-diversity-in-the-species-based-on-cronobacter-genome" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/82396.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">496</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">1260</span> Developing A Novel Fluorescent Sensor For Detecting Analytes In An Aqueous Medium</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Varshith%20Kotagiri">Varshith Kotagiri</a>, <a href="https://publications.waset.org/abstracts/search?q=Lei%20Li"> Lei Li</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Fluorescent sensors are organic fluorophores that detect specific analytes with quantitative fluorescence intensity changes. They have offered impressive benefits compared with instrumental techniques, such as low cost, high selectivity, and rapid responses. One issue that limits the fluorescent sensors for further application is their poor solubility in the aqueous medium, where most targeted analytes, including metal ions, inorganic anions, and neutral biomolecules, are readily soluble. When fluorescent sensors are utilized to detect these analytes, a heterogeneous phase is formed. In most cases, an extra water-miscible organic solvent is needed as an additive to facilitate the sensing process, which complicates the measurement operations and produces more organic waste. We aim to resolve this issue by skillful molecular design to introduce a hydrophilic side chain to the fluorescent sensor, increasing its water solubility and facilitating its sensing process to analytes, like various protons, fluoride ions, and copper ions, in an aqueous medium. Simultaneously, its sensitivity and selectivity will be retained. This work will simplify the sensing operations and reduce the amount of organic waste produced during the measurement. This strategy will additionally be of broad interest to the chemistry community, as it introduces the idea of modifying the molecular structure to apply an initial hydrophobic compound under hydrophilic conditions in a feasible way. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=organic%20fluorescent%20sensor" title="organic fluorescent sensor">organic fluorescent sensor</a>, <a href="https://publications.waset.org/abstracts/search?q=analytes" title=" analytes"> analytes</a>, <a href="https://publications.waset.org/abstracts/search?q=sensing" title=" sensing"> sensing</a>, <a href="https://publications.waset.org/abstracts/search?q=aqueous%20medium" title=" aqueous medium"> aqueous medium</a>, <a href="https://publications.waset.org/abstracts/search?q=phenanthroimidazole" title=" phenanthroimidazole"> phenanthroimidazole</a>, <a href="https://publications.waset.org/abstracts/search?q=hydrophilic%20side%20chain" title=" hydrophilic side chain"> hydrophilic side chain</a> </p> <a href="https://publications.waset.org/abstracts/195039/developing-a-novel-fluorescent-sensor-for-detecting-analytes-in-an-aqueous-medium" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/195039.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">3</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">1259</span> Insights of Interaction Studies between HSP-60, HSP-70 Proteins and HSF-1 in Bubalus bubalis</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Ravinder%20Singh">Ravinder Singh</a>, <a href="https://publications.waset.org/abstracts/search?q=C%20Rajesh"> C Rajesh</a>, <a href="https://publications.waset.org/abstracts/search?q=Saroj%20Badhan"> Saroj Badhan</a>, <a href="https://publications.waset.org/abstracts/search?q=Shailendra%20Mishra"> Shailendra Mishra</a>, <a href="https://publications.waset.org/abstracts/search?q=Ranjit%20Singh%20Kataria"> Ranjit Singh Kataria</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Heat shock protein 60 and 70 are crucial chaperones that guide appropriate folding of denatured proteins under heat stress conditions. HSP60 and HSP70 provide assistance in correct folding of a multitude of denatured proteins. The heat shock factors are the family of some transcription factors which controls the regulation of gene expression of proteins involved in folding of damaged or improper folded proteins during stress conditions. Under normal condition heat shock proteins bind with HSF-1 and act as its repressor as well as aids in maintaining the HSF-1’s nonactive and monomeric confirmation. The experimental protein structure for all these proteins in Bubalus bubalis is not known till date. Therefore computational approach was explored to identify three-dimensional structure analysis of all these proteins. In this study, an extensive in silico analysis has been performed including sequence comparison among species to comparative modeling of Bubalus bubalis HSP60, HSP70 and HSF-1 protein. The stereochemical properties of proteins were assessed by utilizing several scrutiny bioinformatics tools to ensure model accuracy. Further docking approach was used to study interactions between Heat shock proteins and HSF-1. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=Bubalus%20bubalis" title="Bubalus bubalis">Bubalus bubalis</a>, <a href="https://publications.waset.org/abstracts/search?q=comparative%20modelling" title=" comparative modelling"> comparative modelling</a>, <a href="https://publications.waset.org/abstracts/search?q=docking" title=" docking"> docking</a>, <a href="https://publications.waset.org/abstracts/search?q=heat%20shock%20protein" title=" heat shock protein"> heat shock protein</a> </p> <a href="https://publications.waset.org/abstracts/64431/insights-of-interaction-studies-between-hsp-60-hsp-70-proteins-and-hsf-1-in-bubalus-bubalis" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/64431.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">322</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">1258</span> Genetically Encoded Tool with Time-Resolved Fluorescence Readout for the Calcium Concentration Measurement</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Tatiana%20R.%20Simonyan">Tatiana R. Simonyan</a>, <a href="https://publications.waset.org/abstracts/search?q=Elena%20A.%20Protasova"> Elena A. Protasova</a>, <a href="https://publications.waset.org/abstracts/search?q=Anastasia%20V.%20Mamontova"> Anastasia V. Mamontova</a>, <a href="https://publications.waset.org/abstracts/search?q=Eugene%20G.%20Maksimov"> Eugene G. Maksimov</a>, <a href="https://publications.waset.org/abstracts/search?q=Konstantin%20A.%20Lukyanov"> Konstantin A. Lukyanov</a>, <a href="https://publications.waset.org/abstracts/search?q=Alexey%20M.%20Bogdanov"> Alexey M. Bogdanov</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Here, we describe two variants of the calcium indicators based on the GCaMP sensitive core and BrUSLEE fluorescent protein (GCaMP-BrUSLEE and GCaMP-BrUSLEE-145). In contrast to the conventional GCaMP6-family indicators, these fluorophores are characterized by the well-marked responsiveness of their fluorescence decay kinetics to external calcium concentration both in vitro and in cellulo. Specifically, we show that the purified GCaMP-BrUSLEE and GCaMP-BrUSLEE-145 exhibit three-component fluorescence decay kinetics, with the amplitude-normalized lifetime component (t3*A3) of GCaMP-BrUSLEE-145 changing four-fold (500-2000 a.u.) in response to a Ca²⁺ concentration shift in the range of 0—350 nM. Time-resolved fluorescence microscopy of live cells displays the two-fold change of the GCaMP-BrUSLEE-145 mean lifetime upon histamine-stimulated calcium release. The aforementioned Ca²⁺-dependence calls considering the GCaMP-BrUSLEE-145 as a prospective Ca²⁺-indicator with the signal read-out in the time domain. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=calcium%20imaging" title="calcium imaging">calcium imaging</a>, <a href="https://publications.waset.org/abstracts/search?q=fluorescence%20lifetime%20imaging%20microscopy" title=" fluorescence lifetime imaging microscopy"> fluorescence lifetime imaging microscopy</a>, <a href="https://publications.waset.org/abstracts/search?q=fluorescent%20proteins" title=" fluorescent proteins"> fluorescent proteins</a>, <a href="https://publications.waset.org/abstracts/search?q=genetically%20encoded%20indicators" title=" genetically encoded indicators"> genetically encoded indicators</a> </p> <a href="https://publications.waset.org/abstracts/149982/genetically-encoded-tool-with-time-resolved-fluorescence-readout-for-the-calcium-concentration-measurement" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/149982.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">158</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">1257</span> Use RP-HPLC To Investigate Factors Influencing Sorghum Protein Extraction</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Khaled%20Khaladi">Khaled Khaladi</a>, <a href="https://publications.waset.org/abstracts/search?q=Rafika%20Bibi"> Rafika Bibi</a>, <a href="https://publications.waset.org/abstracts/search?q=Hind%20Mokrane"> Hind Mokrane</a>, <a href="https://publications.waset.org/abstracts/search?q=Boubekeur%20Nadjemi"> Boubekeur Nadjemi</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Sorghum (Sorghum bicolor (L.) Moench) is an important cereal crop grown in the semi-arid tropics of Africa and Asia due to its drought tolerance. Sorghum grain has protein content varying from 6 to 18%, with an average of 11%, Sorghum proteins can be broadly classified into prolamin and non-prolamin proteins. Kafirins, the major storage proteins, are classified as prolamins, and as such, they contain high levels of proline and glutamine and are soluble in non-polar solvents such as aqueous alcohols. Kafirins account for 77 to 82% of the protein in the endosperm, whereas non-prolamin proteins (namely, albumins, globulins, and glutelins) make up about 30% of the proteins. To optimize the extraction of sorghum proteins, several variables were examined: detergent type and concentration, reducing agent type and concentration, and buffer pH and concentration. Samples were quantified and characterized by RP-HPLC. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=sorghum" title="sorghum">sorghum</a>, <a href="https://publications.waset.org/abstracts/search?q=protein%20extraction" title=" protein extraction"> protein extraction</a>, <a href="https://publications.waset.org/abstracts/search?q=detergent" title=" detergent"> detergent</a>, <a href="https://publications.waset.org/abstracts/search?q=food%20science" title=" food science "> food science </a> </p> <a href="https://publications.waset.org/abstracts/2669/use-rp-hplc-to-investigate-factors-influencing-sorghum-protein-extraction" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/2669.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">320</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">1256</span> Functional Characterization of Transcriptional Regulator WhiB Proteins of Mycobacterium Tuberculosis</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Sonam%20Kumari">Sonam Kumari</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Mycobacterium tuberculosis (Mtb), the causative agent of tuberculosis, possesses a remarkable feature of entering into and emerging from a persistent state. The mechanism by which Mtb switches from the dormant state to the replicative form is still poorly characterized. Proteome studies have given us an insight into the role of certain proteins in giving stupendous virulence to Mtb, but numerous dotsremain unconnected and unaccounted. The WhiB family of proteins is one such protein that is associated with developmental processes in actinomycetes.Mtb has seven such proteins (WhiB1 to WhiB7).WhiB proteins are transcriptional regulators; their conserved C-terminal HTH motif is involved in DNA binding. They regulate various essential genes of Mtbby binding to their promoter DNA. Biophysical Analysis of the effect of DNA binding on WhiB proteins has not yet been appropriately characterized. Interaction with DNA induces conformational changes in the WhiB proteins, confirmed by steady-state fluorescence and circular dichroism spectroscopy. ITC has deduced thermodynamic parameters and the binding affinity of the interaction. Since these transcription factors are highly unstable in vitro, their stability and solubility were enhanced by the co-expression of molecular chaperones. The present study findings help determine the conditions under which the WhiB proteins interact with their interacting partner and the factors that influence their binding affinity. This is crucial in understanding their role in regulating gene expression in Mtbandin targeting WhiB proteins as a drug target to cure TB. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=tuberculosis" title="tuberculosis">tuberculosis</a>, <a href="https://publications.waset.org/abstracts/search?q=WhiB%20proteins" title=" WhiB proteins"> WhiB proteins</a>, <a href="https://publications.waset.org/abstracts/search?q=mycobacterium%20tuberculosis" title=" mycobacterium tuberculosis"> mycobacterium tuberculosis</a>, <a href="https://publications.waset.org/abstracts/search?q=nucleic%20acid%20binding" title=" nucleic acid binding"> nucleic acid binding</a> </p> <a href="https://publications.waset.org/abstracts/157126/functional-characterization-of-transcriptional-regulator-whib-proteins-of-mycobacterium-tuberculosis" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/157126.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">104</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">1255</span> Effects from Maillard Reactions on the Alleginicity of Peanuts</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Khadija%20Radhi">Khadija Radhi</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Food allergy is a serious public health problem, especially in developed countries. As one of the most significant allergies, peanut allergy was investigated in this research. Peanut was mixed with treacle under different heating conditions. The results of glycation analyses revealed that proteins from peanuts interacted with the carbohydrates. Further studies also indicated that Millard reactions were determined by different heating treatment. It is noted that denatured peanut proteins accelerated the first stage of Millard reactions but prevented the third one. From the ELISA results, it was found that Millard reactions between proteins with sugars had no effects on the allergenicity of peanuts. Besides, there was no significant difference in allergenicity between digested and non-digested peanut proteins. However, pre-boiled peanut with denatured proteins displayed lower allergenicity after mixing with sugars. Such results indicated that denaturation is the key factor to reduce the allergenicity of the peanut proteins and it seemed that the second-staged Maillard products had less allergenicity. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=allergenicity" title="allergenicity">allergenicity</a>, <a href="https://publications.waset.org/abstracts/search?q=heating%20treatment" title=" heating treatment"> heating treatment</a>, <a href="https://publications.waset.org/abstracts/search?q=peanut" title=" peanut"> peanut</a>, <a href="https://publications.waset.org/abstracts/search?q=Maillard%20reaction" title=" Maillard reaction"> Maillard reaction</a> </p> <a href="https://publications.waset.org/abstracts/18275/effects-from-maillard-reactions-on-the-alleginicity-of-peanuts" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/18275.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">333</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">1254</span> Fluorescent Imaging with Hoechst 34580 and Propidium Iodide in Determination of Toxic Changes of Cyanobacterial Oligopeptides in Rotifers</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Adam%20Bownik">Adam Bownik</a>, <a href="https://publications.waset.org/abstracts/search?q=Ma%C5%82gorzata%20Adamczuk"> Małgorzata Adamczuk</a>, <a href="https://publications.waset.org/abstracts/search?q=Barbara%20Pawlik-Skowro%C5%84ska"> Barbara Pawlik-Skowrońska</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Certain strains of cyanobacteria, microorganisms forming water blooms, produce toxic secondary metabolites. Although various effects of cyanotoxins in aquatic animals are known, little data can be found on the influence of some cyanobacterial oligopeptides beyond microcystins. The aim of the present study was to determine the toxicity of novel pure cyanobacterial oligopeptides: microginin FR-1 (MGFR1) and anabaenopeptin-A (ANA-A) on a transparent model rotifer Brachionus calyciflorus with the use of fluorescent double staining with Hoechst 34580 and propidium iodide. The obtained results showed that both studied oligopeptides decreased the fluorescence intensity of animals stained with Hoechst 34580 in a concentration-dependent manner. On the other hand, a concentration-dependent increase of propidium iodide fluorescence was noted in the exposed rotifers. The results suggest that MGFR-1 and ANA-A should be considered as a potent toxic agent to freshwater rotifers, and fluorescent staining with Hoechst and propidium iodide may be a valuable tool for determination of toxicity of cyanobacterial oligopeptides in rotifers. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=cyanobacteria" title="cyanobacteria">cyanobacteria</a>, <a href="https://publications.waset.org/abstracts/search?q=brachionus" title=" brachionus"> brachionus</a>, <a href="https://publications.waset.org/abstracts/search?q=oligopeptides" title=" oligopeptides"> oligopeptides</a>, <a href="https://publications.waset.org/abstracts/search?q=fluorescent%20staining" title=" fluorescent staining"> fluorescent staining</a>, <a href="https://publications.waset.org/abstracts/search?q=hoechst" title=" hoechst"> hoechst</a>, <a href="https://publications.waset.org/abstracts/search?q=propidium%20iodide" title=" propidium iodide"> propidium iodide</a> </p> <a href="https://publications.waset.org/abstracts/146637/fluorescent-imaging-with-hoechst-34580-and-propidium-iodide-in-determination-of-toxic-changes-of-cyanobacterial-oligopeptides-in-rotifers" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/146637.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">130</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">1253</span> Human C-Cbl and Cbl-b Proteins Are More Highly Expressed in the Thymus Compared to the Testis</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Mazo%20Kone">Mazo Kone</a>, <a href="https://publications.waset.org/abstracts/search?q=Rachida%20Salah"> Rachida Salah</a>, <a href="https://publications.waset.org/abstracts/search?q=Harir%20Noria"> Harir Noria</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Background and objectives: c-Cbl and Cbl-b are two members of the Cbl family proteins, with a crucial role of downregulation of tyrosine kinase receptors. They act as E3 ubiquitin ligases and are multivalent adaptor proteins, making them important in maintaining homeostasis in the body. This study investigated the expression level in thymus and testis in normal conditions. Methods: The expression level was assessed by immunochemistry of tissue microarrays of normal thymus and testis biopsies. Results: Cbl-b and c-Cbl proteins were found to be highly expressed in normal testis and thymus, indicated as yellowish brown granules in the cytomembrane and cytoplasm compared to controls. The c-Cbl appears to be more highly expressed than the Cbl-b in the thymus, while c-Cbl appears slightly stronger than Cbl-b in the testis. The thymus was found with a higher grade compared to the testis. Conclusion: In this work we concluded, that in normal condition, thymus tissue expresses more Cbl family proteins(c-Cbl and Cbl-b) than the testis tissue in humans. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=Human%20C-Cbl%20proteins" title="Human C-Cbl proteins">Human C-Cbl proteins</a>, <a href="https://publications.waset.org/abstracts/search?q=Human%20Cbl-b%20protein" title=" Human Cbl-b protein"> Human Cbl-b protein</a>, <a href="https://publications.waset.org/abstracts/search?q=Testis" title=" Testis"> Testis</a>, <a href="https://publications.waset.org/abstracts/search?q=Thymus" title=" Thymus"> Thymus</a> </p> <a href="https://publications.waset.org/abstracts/72064/human-c-cbl-and-cbl-b-proteins-are-more-highly-expressed-in-the-thymus-compared-to-the-testis" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/72064.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">233</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">1252</span> Recovery of Value-Added Whey Proteins from Dairy Effluent Using Aqueous Two-Phase System</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Perumalsamy%20Muthiah">Perumalsamy Muthiah</a>, <a href="https://publications.waset.org/abstracts/search?q=Murugesan%20Thanapalan"> Murugesan Thanapalan</a> </p> <p class="card-text"><strong>Abstract:</strong></p> The remains of cheese production contain nutritional value added proteins viz., α-Lactalbumin, β-Lactoglobulin representing 80- 90% of the total volume of milk entering the process. Although several possibilities for cheese-whey exploitation have been assayed, approximately half of world cheese-whey production is not treated but is discarded as effluent. It is necessary to develop an effective and environmentally benign extraction process for the recovery of value added cheese whey proteins. Recently aqueous two phase system (ATPS) have emerged as potential separation process, particularly in the field of biotechnology due to the mild conditions of the process, short processing time, and ease of scale-up. In order to design an ATPS process for the recovery of cheese whey proteins, development of phase diagram and the effect of system parameters such as pH, types and the concentrations of the phase forming components, temperature, etc., on the partitioning of proteins were addressed in order to maximize the recovery of proteins. Some of the practical problems encountered in the application of aqueous two-phase systems for the recovery of Cheese whey proteins were also discussed. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=aqueous%20two-phase%20system" title="aqueous two-phase system">aqueous two-phase system</a>, <a href="https://publications.waset.org/abstracts/search?q=phase%20diagram" title=" phase diagram"> phase diagram</a>, <a href="https://publications.waset.org/abstracts/search?q=extraction" title=" extraction"> extraction</a>, <a href="https://publications.waset.org/abstracts/search?q=cheese%20whey" title=" cheese whey"> cheese whey</a> </p> <a href="https://publications.waset.org/abstracts/71016/recovery-of-value-added-whey-proteins-from-dairy-effluent-using-aqueous-two-phase-system" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/71016.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">410</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">1251</span> CdS Quantum Dots as Fluorescent Probes for Detection of Naphthalene</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Zhengyu%20Yan">Zhengyu Yan</a>, <a href="https://publications.waset.org/abstracts/search?q=Yan%20Yu"> Yan Yu</a>, <a href="https://publications.waset.org/abstracts/search?q=Jianqiu%20Chen"> Jianqiu Chen</a> </p> <p class="card-text"><strong>Abstract:</strong></p> A novel sensing system has been designed for naphthalene detection based on the quenched fluorescence signal of CdS quantum dots. The fluorescence intensity of the system reduced significantly after adding CdS quantum dots to the water pollution model because of the fluorescent static quenching f mechanism. Herein, we have demonstrated the facile methodology can offer a convenient and low analysis cost with the recovery rate as 97.43%-103.2%, which has potential application prospect. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=CdS%20quantum%20dots" title="CdS quantum dots">CdS quantum dots</a>, <a href="https://publications.waset.org/abstracts/search?q=modification" title=" modification"> modification</a>, <a href="https://publications.waset.org/abstracts/search?q=detection" title=" detection"> detection</a>, <a href="https://publications.waset.org/abstracts/search?q=naphthalene" title=" naphthalene"> naphthalene</a> </p> <a href="https://publications.waset.org/abstracts/10172/cds-quantum-dots-as-fluorescent-probes-for-detection-of-naphthalene" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/10172.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">493</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">1250</span> Study of Aerosol Deposition and Shielding Effects on Fluorescent Imaging Quantitative Evaluation in Protective Equipment Validation</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Shinhao%20Yang">Shinhao Yang</a>, <a href="https://publications.waset.org/abstracts/search?q=Hsiao-Chien%20Huang"> Hsiao-Chien Huang</a>, <a href="https://publications.waset.org/abstracts/search?q=Chin-Hsiang%20Luo"> Chin-Hsiang Luo</a> </p> <p class="card-text"><strong>Abstract:</strong></p> The leakage of protective clothing is an important issue in the occupational health field. There is no quantitative method for measuring the leakage of personal protective equipment. This work aims to measure the quantitative leakage of the personal protective equipment by using the fluorochrome aerosol tracer. The fluorescent aerosols were employed as airborne particulates in a controlled chamber with ultraviolet (UV) light-detectable stickers. After an exposure-and-leakage test, the protective equipment was removed and photographed with UV-scanning to evaluate areas, color depth ratio, and aerosol deposition and shielding effects of the areas where fluorescent aerosols had adhered to the body through the protective equipment. Thus, this work built a calculation software for quantitative leakage ratio of protective clothing based on fluorescent illumination depth/aerosol concentration ratio, illumination/Fa ratio, aerosol deposition and shielding effects, and the leakage area ratio on the segmentation. The results indicated that the two-repetition total leakage rate of the X, Y, and Z type protective clothing for subject T were about 3.05, 4.21, and 3.52 (mg/m2). For five-repetition, the leakage rate of T were about 4.12, 4.52, and 5.11 (mg/m2). <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=fluorochrome" title="fluorochrome">fluorochrome</a>, <a href="https://publications.waset.org/abstracts/search?q=deposition" title=" deposition"> deposition</a>, <a href="https://publications.waset.org/abstracts/search?q=shielding%20effects" title=" shielding effects"> shielding effects</a>, <a href="https://publications.waset.org/abstracts/search?q=digital%20image%20processing" title=" digital image processing"> digital image processing</a>, <a href="https://publications.waset.org/abstracts/search?q=leakage%20ratio" title=" leakage ratio"> leakage ratio</a>, <a href="https://publications.waset.org/abstracts/search?q=personal%20protective%20equipment" title=" personal protective equipment"> personal protective equipment</a> </p> <a href="https://publications.waset.org/abstracts/43218/study-of-aerosol-deposition-and-shielding-effects-on-fluorescent-imaging-quantitative-evaluation-in-protective-equipment-validation" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/43218.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">323</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">1249</span> Novel Fluorescent High Density Polyethylene Composites for Fused Deposition Modeling 3D Printing in Packaging Security Features</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Youssef%20R.%20Hassan">Youssef R. Hassan</a>, <a href="https://publications.waset.org/abstracts/search?q=Mohamed%20S.%20Hasanin"> Mohamed S. Hasanin</a>, <a href="https://publications.waset.org/abstracts/search?q=Reda%20M.%20Abdelhameed"> Reda M. Abdelhameed</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Recently, innovations in packaging security features become more important to see the originality of packaging in industrial application. Luminescent 3d printing materials have been a promising property which can provides a unique opportunity for the design and application of 3D printing. Lack emission of terbium ions, as a source of green emission, in salt form prevent its uses in industrial applications, so searching about stable and highly emitter material become essential. Nowadays, metal organic frameworks (MOFs) play an important role in designing light emitter material. In this work, fluorescent high density polyethylene (FHDPE) composite filament with Tb-benzene 1,3,5-tricarboxylate (Tb-BTC) MOFs for 3D printing have been successfully developed.HDPE pellets were mixed with Tb-BTC and melting extrustion with single screw extruders. It was found that Tb-BTCuniformly dispersed in the HDPE matrix and significantly increased the crystallinity of PE, which not only maintained the good thermal property but also improved the mechanical properties of Tb-BTC@HDPE composites. Notably, the composite filaments emitted ultra-bright green light under UV lamp, and the fluorescence intensity increased as the content of Tb-BTC increased. Finally, several brightly luminescent exquisite articles could be manufactured by fused deposition modeling (FDM) 3D printer with these new fluorescent filaments. In this context, the development of novel fluorescent Tb-BTC@HDPE composites was combined with 3D printing technology to amplified the packaging Security Features. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=3D%20printing" title="3D printing">3D printing</a>, <a href="https://publications.waset.org/abstracts/search?q=fluorescent" title=" fluorescent"> fluorescent</a>, <a href="https://publications.waset.org/abstracts/search?q=packaging" title=" packaging"> packaging</a>, <a href="https://publications.waset.org/abstracts/search?q=security" title=" security"> security</a> </p> <a href="https://publications.waset.org/abstracts/158294/novel-fluorescent-high-density-polyethylene-composites-for-fused-deposition-modeling-3d-printing-in-packaging-security-features" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/158294.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">101</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">1248</span> Proteomic Analysis of Excretory Secretory Antigen (ESA) from Entamoeba histolytica HM1: IMSS</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=N.%20Othman">N. Othman</a>, <a href="https://publications.waset.org/abstracts/search?q=J.%20Ujang"> J. Ujang</a>, <a href="https://publications.waset.org/abstracts/search?q=M.%20N.%20Ismail"> M. N. Ismail</a>, <a href="https://publications.waset.org/abstracts/search?q=R.%20Noordin"> R. Noordin</a>, <a href="https://publications.waset.org/abstracts/search?q=B.%20H.%20Lim"> B. H. Lim</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Amoebiasis is caused by the Entamoeba histolytica and still endemic in many parts of the tropical region, worldwide. Currently, there is no available vaccine against amoebiasis. Hence, there is an urgent need to develop a vaccine. The excretory secretory antigen (ESA) of E. histolytica is a suitable biomarker for the vaccine candidate since it can modulate the host immune response. Hence, the objective of this study is to identify the proteome of the ESA towards finding suitable biomarker for the vaccine candidate. The non-gel based and gel-based proteomics analyses were performed to identify proteins. Two kinds of mass spectrometry with different ionization systems were utilized i.e. LC-MS/MS (ESI) and MALDI-TOF/TOF. Then, the functional proteins classification analysis was performed using PANTHER software. Combination of the LC -MS/MS for the non-gel based and MALDI-TOF/TOF for the gel-based approaches identified a total of 273 proteins from the ESA. Both systems identified 29 similar proteins whereby 239 and 5 more proteins were identified by LC-MS/MS and MALDI-TOF/TOF, respectively. Functional classification analysis showed the majority of proteins involved in the metabolic process (24%), primary metabolic process (19%) and protein metabolic process (10%). Thus, this study has revealed the proteome the E. histolytica ESA and the identified proteins merit further investigations as a vaccine candidate. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=E.%20histolytica" title="E. histolytica">E. histolytica</a>, <a href="https://publications.waset.org/abstracts/search?q=ESA" title=" ESA"> ESA</a>, <a href="https://publications.waset.org/abstracts/search?q=proteomics" title=" proteomics"> proteomics</a>, <a href="https://publications.waset.org/abstracts/search?q=biomarker" title=" biomarker "> biomarker </a> </p> <a href="https://publications.waset.org/abstracts/34707/proteomic-analysis-of-excretory-secretory-antigen-esa-from-entamoeba-histolytica-hm1-imss" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/34707.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">1247</span> A Turn-on Fluorescent Sensor for Pb(II)</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Ece%20K%C3%B6k%20Yetimo%C4%9Flu">Ece Kök Yetimoğlu</a>, <a href="https://publications.waset.org/abstracts/search?q=Soner%20%C3%87ubuk"> Soner Çubuk</a>, <a href="https://publications.waset.org/abstracts/search?q=Ne%C5%9Fe%20Ta%C5%9Fci"> Neşe Taşci</a>, <a href="https://publications.waset.org/abstracts/search?q=M.%20Vezir%20Kahraman"> M. Vezir Kahraman</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Lead(II) is one of the most toxic environmental pollutants in the world, due to its high toxicity and non-biodegradability. Lead exposure causes severe risks to human health such as central brain damages, convulsions, kidney damages, and even death. To determine lead(II) in environmental or biological samples, scientists use atomic absorption spectrometry (AAS), inductively coupled plasma mass spectrometry (ICPMS), fluorescence spectrometry and electrochemical techniques. Among these systems the fluorescence spectrometry and fluorescent chemical sensors have attracted considerable attention because of their good selectivity and high sensitivity. The fluorescent polymers usually contain covalently bonded fluorophores. In this study imidazole based UV cured polymeric film was prepared and designed to act as a fluorescence chemo sensor for lead (II) analysis. The optimum conditions such as influence of pH value and time on the fluorescence intensity of the sensor have also been investigated. The sensor was highly sensitive with a detection limit as low as 1.87 × 10−8 mol L-1 and it was successful in the determination of Pb(II) in water samples. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=fluorescence" title="fluorescence">fluorescence</a>, <a href="https://publications.waset.org/abstracts/search?q=lead%28II%29" title=" lead(II)"> lead(II)</a>, <a href="https://publications.waset.org/abstracts/search?q=photopolymerization" title=" photopolymerization"> photopolymerization</a>, <a href="https://publications.waset.org/abstracts/search?q=polymeric%20sensor" title=" polymeric sensor"> polymeric sensor</a> </p> <a href="https://publications.waset.org/abstracts/46887/a-turn-on-fluorescent-sensor-for-pbii" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/46887.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">671</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">1246</span> An Insight into the Interaction Study of a WhiB Protein and its Binding Partner</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Sonam%20Kumari">Sonam Kumari</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Tuberculosis is the deadliest disease worldwide. Millions of people lose their lives every year due to this disease. It has turned lethal due to the erratic nature of its causative organism, Mycobacterium tuberculosis (Mtb). Mtb tends to enter into an inactive, dormant state and emerge to replicating state upon encountering favorable conditions. The mechanism by which Mtb switches from the dormant state to the replicative form is still poorly characterized. Proteome studies have given us an insight into the role of certain proteins in giving stupendous virulence to Mtb, but numerous dotsremain unconnected and unaccounted. The WhiB family of proteins is one such protein that is associated with developmental processes in actinomycetes. Mtb has seven such proteins (WhiB1 to WhiB7). WhiB proteins are transcriptional regulators; they regulate various essential genes of Mtbby binding to their promoter DNA. Biophysical parameters of the effect of DNA binding on WhiB proteins has not yet been appropriately characterized. Interaction with DNA induces conformational changes in the WhiB proteins, confirmed by steady-state fluorescence and circular dichroism spectroscopy. ITC has deduced thermodynamic parameters and the binding affinity of the interaction. Since these transcription factors are highly unstable in vitro, their stability and solubility were enhanced by the co-expression of molecular chaperones. The present study findings help determine the conditions under which the WhiB proteins interact with their interacting partner and the factors that influence their binding affinity. This is crucial in understanding their role in regulating gene expression in Mtbandin targeting WhiB proteins as a drug target to cure TB. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=mycobacterium%20tuberculosis" title="mycobacterium tuberculosis">mycobacterium tuberculosis</a>, <a href="https://publications.waset.org/abstracts/search?q=TB" title=" TB"> TB</a>, <a href="https://publications.waset.org/abstracts/search?q=whiB%20proteins" title=" whiB proteins"> whiB proteins</a>, <a href="https://publications.waset.org/abstracts/search?q=ITC" title=" ITC"> ITC</a> </p> <a href="https://publications.waset.org/abstracts/157140/an-insight-into-the-interaction-study-of-a-whib-protein-and-its-binding-partner" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/157140.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">97</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">1245</span> Functionalization of Carbon-Coated Iron Nanoparticles with Fluorescent Protein</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=A.%20G.%20Pershina">A. G. Pershina</a>, <a href="https://publications.waset.org/abstracts/search?q=P.%20S.%20Postnikov"> P. S. Postnikov</a>, <a href="https://publications.waset.org/abstracts/search?q=M.%20E.%20Trusova"> M. E. Trusova</a>, <a href="https://publications.waset.org/abstracts/search?q=D.%20O.%20Burlakova"> D. O. Burlakova</a>, <a href="https://publications.waset.org/abstracts/search?q=A.%20E.%20Sazonov"> A. E. Sazonov</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Invention of magnetic-fluorescent nanocomposites is a rapidly developing area of research. The magnetic-fluorescent nanocomposite attractiveness is connected with the ability of simultaneous management and control of such nanocomposites by two independent methods based on different physical principles. These nanocomposites are applied for the solution of various essential scientific and experimental biomedical problems. The aim of this research is development of principle approach to nanobiohybrid structures with magnetic and fluorescent properties design. The surface of carbon-coated iron nanoparticles (Fe@C) were covalently modified by 4-carboxy benzenediazonium tosylate. Recombinant fluorescent protein TagGFP2 (Eurogen) was obtained in E. coli (Rosetta DE3) by standard laboratory techniques. Immobilization of TagGFP2 on the nanoparticles surface was provided by the carbodiimide activation. The amount of COOH-groups on the nanoparticle surface was estimated by elemental analysis (Elementar Vario Macro) and TGA-analysis (SDT Q600, TA Instruments. Obtained nanocomposites were analyzed by FTIR spectroscopy (Nicolet Thermo 5700) and fluorescence microscopy (AxioImager M1, Carl Zeiss). Amount of the protein immobilized on the modified nanoparticle surface was determined by fluorimetry (Cary Eclipse) and spectrophotometry (Unico 2800) with the help of preliminary obtained calibration plots. In the FTIR spectra of modified nanoparticles the adsorption band of –COOH group around 1700 cm-1 and bands in the region of 450-850 cm-1 caused by bending vibrations of benzene ring were observed. The calculated quantity of active groups on the surface was equal to 0,1 mmol/g of material. The carbodiimide activation of COOH-groups on nanoparticles surface results to covalent immobilization of TagGFP2 fluorescent protein (0.2 nmol/mg). The success of immobilization was proved by FTIR spectroscopy. Protein characteristic adsorption bands in the region of 1500-1600 cm-1 (amide I) were presented in the FTIR spectrum of nanocomposite. The fluorescence microscopy analysis shows that Fe@C-TagGFP2 nanocomposite possesses fluorescence properties. This fact confirms that TagGFP2 protein retains its conformation due to immobilization on nanoparticles surface. Magnetic-fluorescent nanocomposite was obtained as a result of unique design solution implementation – the fluorescent protein molecules were fixed to the surface of superparamagnetic carbon-coated iron nanoparticles using original diazonium salts. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=carbon-coated%20iron%20nanoparticles" title="carbon-coated iron nanoparticles">carbon-coated iron nanoparticles</a>, <a href="https://publications.waset.org/abstracts/search?q=diazonium%20salts" title=" diazonium salts"> diazonium salts</a>, <a href="https://publications.waset.org/abstracts/search?q=fluorescent%20protein" title=" fluorescent protein"> fluorescent protein</a>, <a href="https://publications.waset.org/abstracts/search?q=immobilization" title=" immobilization"> immobilization</a> </p> <a href="https://publications.waset.org/abstracts/7691/functionalization-of-carbon-coated-iron-nanoparticles-with-fluorescent-protein" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/7691.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">342</span> </span> </div> </div> <ul class="pagination"> <li class="page-item disabled"><span class="page-link">&lsaquo;</span></li> <li class="page-item active"><span class="page-link">1</span></li> <li class="page-item"><a class="page-link" href="https://publications.waset.org/abstracts/search?q=fluorescent%20proteins&page=2">2</a></li> <li class="page-item"><a class="page-link" href="https://publications.waset.org/abstracts/search?q=fluorescent%20proteins&page=3">3</a></li> <li class="page-item"><a class="page-link" href="https://publications.waset.org/abstracts/search?q=fluorescent%20proteins&page=4">4</a></li> <li class="page-item"><a class="page-link" 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