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docking</title> <meta name="description" content="Search results for: molecular docking"> <meta name="keywords" content="molecular docking"> <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="molecular docking"> <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> 2174</div> </div> </div> </div> <h1 class="mt-3 mb-3 text-center" style="font-size:1.6rem;">Search results for: molecular docking</h1> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">2174</span> Molecular Docking Assessment of Pesticides Binding to Bacterial Chitinases</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Diana%20Larisa%20Vladoiu">Diana Larisa Vladoiu</a>, <a href="https://publications.waset.org/abstracts/search?q=Vasile%20Ostafe"> Vasile Ostafe</a>, <a href="https://publications.waset.org/abstracts/search?q=Adriana%20Isvoran"> Adriana Isvoran</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Molecular docking calculations reveal that pesticides provide favorable interactions with the bacterial chitinases. Pesticides interact with both hydrophilic and aromatic residues involved in the active site of the enzymes, their positions partially overlapping the substrate and the inhibitors locations. Molecular docking outcomes, in correlation with experimental literature data, suggest that the pesticides may be degraded or having an inhibitor effect on the activity of these enzymes, depending of the application dose and rate. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=chitinases" title="chitinases">chitinases</a>, <a href="https://publications.waset.org/abstracts/search?q=inhibition" title=" inhibition"> inhibition</a>, <a href="https://publications.waset.org/abstracts/search?q=molecular%20docking" title=" molecular docking"> molecular docking</a>, <a href="https://publications.waset.org/abstracts/search?q=pesticides" title=" pesticides"> pesticides</a> </p> <a href="https://publications.waset.org/abstracts/25456/molecular-docking-assessment-of-pesticides-binding-to-bacterial-chitinases" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/25456.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">551</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">2173</span> Microbiological Activity and Molecular Docking Study of Selected Steroid Derivatives of Biomedical Importance</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Milica%20Karadzic">Milica Karadzic</a>, <a href="https://publications.waset.org/abstracts/search?q=Lidija%20Jevric"> Lidija Jevric</a>, <a href="https://publications.waset.org/abstracts/search?q=Sanja%20Podunavac-Kuzmanovic"> Sanja Podunavac-Kuzmanovic</a>, <a href="https://publications.waset.org/abstracts/search?q=Strahinja%20Kovacevic"> Strahinja Kovacevic</a>, <a href="https://publications.waset.org/abstracts/search?q=Sinisa%20Markov"> Sinisa Markov</a>, <a href="https://publications.waset.org/abstracts/search?q=Aleksandar%20Okljesa"> Aleksandar Okljesa</a>, <a href="https://publications.waset.org/abstracts/search?q=Andrea%20Nikolic"> Andrea Nikolic</a>, <a href="https://publications.waset.org/abstracts/search?q=Marija%20Sakac"> Marija Sakac</a>, <a href="https://publications.waset.org/abstracts/search?q=Katarina%20Penov%20Gasi"> Katarina Penov Gasi</a> </p> <p class="card-text"><strong>Abstract:</strong></p> This study considered the microbiological activity determination and molecular docking study for selected steroid derivatives of biomedical importance. Minimal inhibitory concentration (MIC) was determined for steroid derivatives against Staphylococcus aureus using macrodilution method. Some of the investigated steroid derivatives express bacteriostatic effect against Staphylococcus aureus. Molecular docking approaches are the most widely used techniques for predicting the binding mode of a ligand. Molecular docking study was done for steroid derivatives for androgen receptor negative prostate cancer cell line (PC-3) toward Human Cytochrome P450 CYP17A1. The molecules that had the smallest experimental IC50 values confirmed their ability to dock into active place using suitable molecular docking procedure. The binding disposition of those molecules was thoroughly investigated. Microbiological analysis and molecular docking study were conducted with aim to additionally characterize selected steroid derivatives for future investigation regarding their biological activity and to estimate the binding-affinities of investigated derivatives. This article is based upon work from COST Action (TD1305), supported by COST (European Cooperation and Science and Technology). <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=binding%20affinity" title="binding affinity">binding affinity</a>, <a href="https://publications.waset.org/abstracts/search?q=minimal%20inhibitory%20concentration" title=" minimal inhibitory concentration"> minimal inhibitory concentration</a>, <a href="https://publications.waset.org/abstracts/search?q=molecular%20docking" title=" molecular docking"> molecular docking</a>, <a href="https://publications.waset.org/abstracts/search?q=pc-3%20cell%20line" title=" pc-3 cell line"> pc-3 cell line</a>, <a href="https://publications.waset.org/abstracts/search?q=staphylococcus%20aureus" title=" staphylococcus aureus"> staphylococcus aureus</a>, <a href="https://publications.waset.org/abstracts/search?q=steroids" title=" steroids"> steroids</a> </p> <a href="https://publications.waset.org/abstracts/60204/microbiological-activity-and-molecular-docking-study-of-selected-steroid-derivatives-of-biomedical-importance" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/60204.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">365</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">2172</span> Molecular Docking Study of Quinazoline and Quinoline Derivatives against EGFR</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Asli%20Faiza">Asli Faiza</a>, <a href="https://publications.waset.org/abstracts/search?q=Khamouli%20Saida"> Khamouli Saida</a> </p> <p class="card-text"><strong>Abstract:</strong></p> With the development of computer tools over the past 20 years. Molecular modeling and, more precisely, molecular docking has very quickly entered field of pharmaceutical research. EGFR enzyme involved in cancer disease.Our work consists of studying the inhibition of EGFR (1M17) with deferent inhibitors derived from quinazoline and quinoline by molecular docking. The values of ligands L148 and L177 are the best ligands for inhibit the activity of 1M17 since it forms a stable complex with this enzyme by better binding to the active site. The results obtained show that the ligands L148 and L177 give weak interactions with the active site residues EGFR (1M17), which stabilize the complexes formed of this ligands, which gives a better binding at the level of the active site, and an RMSD of L148 [1,9563 Å] and of L177 [ 1,2483 Å]. [1, 9563, 1.2483] Å <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=docking" title="docking">docking</a>, <a href="https://publications.waset.org/abstracts/search?q=EGFR" title=" EGFR"> EGFR</a>, <a href="https://publications.waset.org/abstracts/search?q=quinazoline" title=" quinazoline"> quinazoline</a>, <a href="https://publications.waset.org/abstracts/search?q=quinoli%C3%A8ne" title=" quinoliène"> quinoliène</a>, <a href="https://publications.waset.org/abstracts/search?q=MOE" title=" MOE"> MOE</a> </p> <a href="https://publications.waset.org/abstracts/176733/molecular-docking-study-of-quinazoline-and-quinoline-derivatives-against-egfr" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/176733.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">68</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">2171</span> The Effect of Sorafenibe on Soat1 Protein by Using Molecular Docking Method</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Mahdiyeh%20Gholaminezhad">Mahdiyeh Gholaminezhad</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Context: The study focuses on the potential impact of Sorafenib on SOAT1 protein in liver cancer treatment, addressing the need for more effective therapeutic options. Research aim: To explore the effects of Sorafenib on the activity of SOAT1 protein in liver cancer cells. Methodology: Molecular docking was employed to analyze the interaction between Sorafenib and SOAT1 protein. Findings: The study revealed a significant effect of Sorafenib on the stability and activity of SOAT1 protein, suggesting its potential as a treatment for liver cancer. Theoretical importance: This research highlights the molecular mechanism underlying Sorafenib's anti-cancer properties, contributing to the understanding of its therapeutic effects. Data collection: Data on the molecular structure of Sorafenib and SOAT1 protein were obtained from computational simulations and databases. Analysis procedures: Molecular docking simulations were performed to predict the binding interactions between Sorafenib and SOAT1 protein. Question addressed: How does Sorafenib influence the activity of SOAT1 protein and what are the implications for liver cancer treatment? Conclusion: The study demonstrates the potential of Sorafenib as a targeted therapy for liver cancer by affecting the activity of SOAT1 protein. Reviewers' Comments: The study provides valuable insights into the molecular basis of Sorafenib's action on SOAT1 protein, suggesting its therapeutic potential. To enhance the methodology, the authors could consider validating the docking results with experimental data for further validation. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=liver%20cancer" title="liver cancer">liver cancer</a>, <a href="https://publications.waset.org/abstracts/search?q=sorafenib" title=" sorafenib"> sorafenib</a>, <a href="https://publications.waset.org/abstracts/search?q=SOAT1" title=" SOAT1"> SOAT1</a>, <a href="https://publications.waset.org/abstracts/search?q=molecular%20docking" title=" molecular docking"> molecular docking</a> </p> <a href="https://publications.waset.org/abstracts/189263/the-effect-of-sorafenibe-on-soat1-protein-by-using-molecular-docking-method" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/189263.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">26</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">2170</span> Synthesis and Molecular Docking of Isonicotinohydrazide Derivatives as Anti-Tuberculosis Candidates</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Ruswanto%20Ruswanto">Ruswanto Ruswanto</a>, <a href="https://publications.waset.org/abstracts/search?q=Richa%20Mardianingrum"> Richa Mardianingrum</a>, <a href="https://publications.waset.org/abstracts/search?q=Tita%20Nofianti"> Tita Nofianti</a>, <a href="https://publications.waset.org/abstracts/search?q=Nur%20Rahayuningsih"> Nur Rahayuningsih</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Tuberculosis (TB) is a chronic disease as a result of Mycobacterium tuberculosis. It can affect all age groups, and hence, is a global health problem that causes the death of millions of people every year. One of the drugs used in tuberculosis treatment is isonicotinohydrazide. In this study, N'-benzoylisonicotinohydrazide derivative compounds (a-l) were prepared using acylation reactions between isonicotinohydrazide and benzoyl chloride derivatives, through the reflux method. Molecular docking studies suggested that all of the compounds had better interaction with Mycobacterium tuberculosis enoyl-acyl carrier protein reductase (InhA) than isonicotinohydrazide. It can be concluded that N'-benzoylisonicotinohydrazide derivatives (a-l) could be used as anti-tuberculosis candidates. From the docking results revealed that all of the compounds interact well with InhA, with compound g (N'-(3-nitrobenzoyl)isonicotinohydrazide) exhibiting the best interaction. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=anti-tuberculosis" title="anti-tuberculosis ">anti-tuberculosis </a>, <a href="https://publications.waset.org/abstracts/search?q=docking" title=" docking"> docking</a>, <a href="https://publications.waset.org/abstracts/search?q=InhA" title=" InhA"> InhA</a>, <a href="https://publications.waset.org/abstracts/search?q=N%27-benzoylisonicotinohydrazide" title=" N'-benzoylisonicotinohydrazide"> N'-benzoylisonicotinohydrazide</a>, <a href="https://publications.waset.org/abstracts/search?q=synthesis" title=" synthesis"> synthesis</a> </p> <a href="https://publications.waset.org/abstracts/91333/synthesis-and-molecular-docking-of-isonicotinohydrazide-derivatives-as-anti-tuberculosis-candidates" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/91333.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">310</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">2169</span> Enzyme Inhibition Activity of Schiff Bases Against Mycobacterium Tuberculosis Using Molecular Docking</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Imran%20Muhammad">Imran Muhammad</a> </p> <p class="card-text"><strong>Abstract:</strong></p> The main cause of infectious disease in the modern world is Mycobacterium Tuberculosis (MT). To combat tuberculosis, new and efficient drugs are an urgent need in the modern world. Schif bases are potent for their biological pharmacophore activity. Thus we selected different Vanillin-based Schiff bases for their binding activity against target enzymes of Mycobacterium tuberculosis that is (DprE1 (decaprenyl phosphoryl-β-D-ribose 2′-epimerase), and DNA gyrase subunit-A), using molecular docking. We evaluate the inhibition potential, interaction, and binding mode of these compounds with the target enzymes. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=schiff%20bases" title="schiff bases">schiff bases</a>, <a href="https://publications.waset.org/abstracts/search?q=tuberculosis" title=" tuberculosis"> tuberculosis</a>, <a href="https://publications.waset.org/abstracts/search?q=DNA%20gyrase" title=" DNA gyrase"> DNA gyrase</a>, <a href="https://publications.waset.org/abstracts/search?q=DprE1" title=" DprE1"> DprE1</a>, <a href="https://publications.waset.org/abstracts/search?q=docking" title=" docking"> docking</a> </p> <a href="https://publications.waset.org/abstracts/168664/enzyme-inhibition-activity-of-schiff-bases-against-mycobacterium-tuberculosis-using-molecular-docking" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/168664.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">75</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">2168</span> Structure-Based Virtual Screening to Identify CLDN4 Inhibitors</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Jayanthi%20Sivaraman">Jayanthi Sivaraman</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Claudins are the important components of the tight junctions that play a key role in paracellular permeability. Among various members of Claudin family, Claudin 4 (CLDN4) is found to be overexpressed in ovarian, pancreatic carcinomas and other epithelial malignancies. Therefore, in this study, an attempt has been made to identify potent inhibitors for CLDN4 from the ZINC database using virtual screening, molecular docking and molecular dynamics simulations. A well refined molecular model of CLDN4 was built using Prime of Schrodinger v10.2(Template- PDB ID: 4P79). Approximately, 6 million compounds from ZINC database are subjected to high-throughput virtual screening (HTVS) against the active site of CLDN4. Molecular docking using GLIDE predicted ARG31, ASN142, ASP146 and ARG158 as critically important residues. Furthermore, three compounds from ZINC database (ZINC96331839, ZINC36533519 and ZINC75819394) showed highly promising ADME properties and binding affinity with stable conformation. The therapeutic efficiency of these lead compounds is evaluated and confirmed by in-vitro and in-vivo studies which leads to the development of novel anti-cancer drugs. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=ADME%20property" title="ADME property">ADME property</a>, <a href="https://publications.waset.org/abstracts/search?q=inhibitors" title=" inhibitors"> inhibitors</a>, <a href="https://publications.waset.org/abstracts/search?q=molecular%20docking" title=" molecular docking"> molecular docking</a>, <a href="https://publications.waset.org/abstracts/search?q=virtual%20screening" title=" virtual screening"> virtual screening</a> </p> <a href="https://publications.waset.org/abstracts/56042/structure-based-virtual-screening-to-identify-cldn4-inhibitors" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/56042.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">2167</span> Molecular Docking and Synthesis of Nitrogen-Containing Bisphosphonates </h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=S.%20Ghalem">S. Ghalem</a>, <a href="https://publications.waset.org/abstracts/search?q=M.%20Mesmoudi"> M. Mesmoudi</a>, <a href="https://publications.waset.org/abstracts/search?q=I.%20Daoudand"> I. Daoudand</a>, <a href="https://publications.waset.org/abstracts/search?q=H.%20Allali"> H. Allali</a> </p> <p class="card-text"><strong>Abstract:</strong></p> The nitrogen-containing bisphosphonates (N-BPs) are well established as the treatments of choice for disorders of excessive bone resorption, myeloma and bone metastases, and osteoporosis. They inhibit farnesyl pyrophosphate synthase (FFPS), a key enzyme in the mevalonate pathway, resulting in inhibition of the prenylation of small GTP-binding proteins in osteoclasts and disruption of their cytoskeleton, adhesion/spreading, and invasion of cancer cells. A very few examples for synthesis of α-amino bisphosphonates based on several amino acids are known from the literature. In the present work, esters of aminoacid react with ketophsophonate (or their analog acid or acyl) to afford the desired products, α-iminophosphonates. The reaction of imine with dimethyl phosphate in the presence of catalytic amount of I2 give ester of α-aminobisphosphonate as sole product in good yield. Finally, we used computational docking methods to predict how several α-aminobisphosphonates bind to FPPS and how R and X influence. Pamidronate, β-aminobisphosphonate already marketed, was used as reference. These results are of interest since they represent a new and simple way to sythesize α-aminobisphosphonates with a free COOH group increased by R2 functionalisable and opening up the possibility of using the molecular docking to facilitate the design of other, novel FFPS inhibitors. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=drug%20research" title="drug research">drug research</a>, <a href="https://publications.waset.org/abstracts/search?q=cancer" title=" cancer"> cancer</a>, <a href="https://publications.waset.org/abstracts/search?q=%CE%B1-amino%20bisphosphonates" title=" α-amino bisphosphonates"> α-amino bisphosphonates</a>, <a href="https://publications.waset.org/abstracts/search?q=molecular%20docking" title=" molecular docking"> molecular docking</a> </p> <a href="https://publications.waset.org/abstracts/43154/molecular-docking-and-synthesis-of-nitrogen-containing-bisphosphonates" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/43154.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">271</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">2166</span> In-silico DFT Study, Molecular Docking, ADMET Predictions, and DMS of Isoxazolidine and Isoxazoline Analogs with Anticancer Properties</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Moulay%20Driss%20Mellaoui">Moulay Driss Mellaoui</a>, <a href="https://publications.waset.org/abstracts/search?q=Khadija%20Zaki"> Khadija Zaki</a>, <a href="https://publications.waset.org/abstracts/search?q=Khalid%20Abbiche"> Khalid Abbiche</a>, <a href="https://publications.waset.org/abstracts/search?q=Abdallah%20Imjjad"> Abdallah Imjjad</a>, <a href="https://publications.waset.org/abstracts/search?q=Rachid%20Boutiddar"> Rachid Boutiddar</a>, <a href="https://publications.waset.org/abstracts/search?q=Abdelouahid%20Sbai"> Abdelouahid Sbai</a>, <a href="https://publications.waset.org/abstracts/search?q=Aaziz%20Jmiai"> Aaziz Jmiai</a>, <a href="https://publications.waset.org/abstracts/search?q=Souad%20El%20Issami"> Souad El Issami</a>, <a href="https://publications.waset.org/abstracts/search?q=Al%20Mokhtar%20Lamsabhi"> Al Mokhtar Lamsabhi</a>, <a href="https://publications.waset.org/abstracts/search?q=Hanane%20Zejli"> Hanane Zejli</a> </p> <p class="card-text"><strong>Abstract:</strong></p> This study presents a comprehensive analysis of six isoxazolidine and isoxazoline derivatives, leveraging a multifaceted approach that combines Density Functional Theory (DFT), AdmetSAR analysis, and molecular docking simulations to explore their electronic, pharmacokinetic, and anticancer properties. Through DFT analysis, using the B3LYP-D3BJ functional and the 6-311++G(d,p) basis set, we optimized molecular geometries, analyzed vibrational frequencies, and mapped Molecular Electrostatic Potentials (MEP), identifying key sites for electrophilic attacks and hydrogen bonding. Frontier Molecular Orbital (FMO) analysis and Density of States (DOS) plots revealed varying stability levels among the compounds, with 1b, 2b, and 3b showing slightly higher stability. Chemical potential assessments indicated differences in binding affinities, suggesting stronger potential interactions for compounds 1b and 2b. AdmetSAR analysis predicted favorable human intestinal absorption (HIA) rates for all compounds, highlighting compound 3b superior oral effectiveness. Molecular docking and molecular dynamics simulations were conducted on isoxazolidine and 4-isoxazoline derivatives targeting the EGFR receptor (PDB: 1JU6). Molecular docking simulations confirmed the high affinity of these compounds towards the target protein 1JU6, particularly compound 3b, among the isoxazolidine derivatives, compound 3b exhibited the most favorable binding energy, with a g score of -8.50 kcal/mol. Molecular dynamics simulations over 100 nanoseconds demonstrated the stability and potential of compound 3b as a superior candidate for anticancer applications, further supported by structural analyses including RMSD, RMSF, Rg, and SASA values. This study underscores the promising role of compound 3b in anticancer treatments, providing a solid foundation for future drug development and optimization efforts. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=isoxazolines" title="isoxazolines">isoxazolines</a>, <a href="https://publications.waset.org/abstracts/search?q=DFT" title=" DFT"> DFT</a>, <a href="https://publications.waset.org/abstracts/search?q=molecular%20docking" title=" molecular docking"> molecular docking</a>, <a href="https://publications.waset.org/abstracts/search?q=molecular%20dynamic" title=" molecular dynamic"> molecular dynamic</a>, <a href="https://publications.waset.org/abstracts/search?q=ADMET" title=" ADMET"> ADMET</a>, <a href="https://publications.waset.org/abstracts/search?q=drugs." title=" drugs."> drugs.</a> </p> <a href="https://publications.waset.org/abstracts/186194/in-silico-dft-study-molecular-docking-admet-predictions-and-dms-of-isoxazolidine-and-isoxazoline-analogs-with-anticancer-properties" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/186194.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">47</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">2165</span> QSAR, Docking and E-pharmacophore Approach on Novel Series of HDAC Inhibitors with Thiophene Linker as Anticancer Agents</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Harish%20Rajak">Harish Rajak</a>, <a href="https://publications.waset.org/abstracts/search?q=Preeti%20Patel"> Preeti Patel</a> </p> <p class="card-text"><strong>Abstract:</strong></p> HDAC inhibitors can reactivate gene expression and inhibit the growth and survival of cancer cells. The 3D-QSAR and Pharmacophore modeling studies were performed to identify important pharmacophoric features and correlate 3D-chemical structure with biological activity. The pharmacophore hypotheses were developed using e-pharmacophore script and phase module. Pharmacophore hypothesis represents the 3D arrangement of molecular features necessary for activity. A series of 55 compounds with well-assigned HDAC inhibitory activity was used for 3D-QSAR model development. Best 3D-QSAR model, which is a five PLS factor model with good statistics and predictive ability, acquired Q2 (0.7293), R2 (0.9811) and standard deviation (0.0952). Molecular docking were performed using Histone Deacetylase protein (PDB ID: 1t69) and prepared series of hydroxamic acid based HDAC inhibitors. Docking study of compound 43 show significant binding interactions Ser 276 and oxygen atom of dioxine cap region, Gly 151 and amino group and Asp 267 with carboxyl group of CONHOH, which are essential for anticancer activity. On docking, most of the compounds exhibited better glide score values between -8 to -10.5. We have established structure activity correlation using docking, energetic based pharmacophore modelling, pharmacophore and atom based 3D QSAR model. The results of these studies were further used for the design and testing of new HDAC analogs. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=Docking" title="Docking">Docking</a>, <a href="https://publications.waset.org/abstracts/search?q=e-pharmacophore" title=" e-pharmacophore"> e-pharmacophore</a>, <a href="https://publications.waset.org/abstracts/search?q=HDACIs" title=" HDACIs"> HDACIs</a>, <a href="https://publications.waset.org/abstracts/search?q=QSAR" title=" QSAR"> QSAR</a>, <a href="https://publications.waset.org/abstracts/search?q=Suberoylanilidehydroxamic%20acid." title=" Suberoylanilidehydroxamic acid."> Suberoylanilidehydroxamic acid.</a> </p> <a href="https://publications.waset.org/abstracts/40734/qsar-docking-and-e-pharmacophore-approach-on-novel-series-of-hdac-inhibitors-with-thiophene-linker-as-anticancer-agents" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/40734.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">301</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">2164</span> Exploring 1,2,4-Triazine-3(2H)-One Derivatives as Anticancer Agents for Breast Cancer: A QSAR, Molecular Docking, ADMET, and Molecular Dynamics</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Said%20Belaaouad">Said Belaaouad</a> </p> <p class="card-text"><strong>Abstract:</strong></p> This study aimed to explore the quantitative structure-activity relationship (QSAR) of 1,2,4-Triazine-3(2H)-one derivative as a potential anticancer agent against breast cancer. The electronic descriptors were obtained using the Density Functional Theory (DFT) method, and a multiple linear regression techniques was employed to construct the QSAR model. The model exhibited favorable statistical parameters, including R2=0.849, R2adj=0.656, MSE=0.056, R2test=0.710, and Q2cv=0.542, indicating its reliability. Among the descriptors analyzed, absolute electronegativity (χ), total energy (TE), number of hydrogen bond donors (NHD), water solubility (LogS), and shape coefficient (I) were identified as influential factors. Furthermore, leveraging the validated QSAR model, new derivatives of 1,2,4-Triazine-3(2H)-one were designed, and their activity and pharmacokinetic properties were estimated. Subsequently, molecular docking (MD) and molecular dynamics (MD) simulations were employed to assess the binding affinity of the designed molecules. The Tubulin colchicine binding site, which plays a crucial role in cancer treatment, was chosen as the target protein. Through the simulation trajectory spanning 100 ns, the binding affinity was calculated using the MMPBSA script. As a result, fourteen novel Tubulin-colchicine inhibitors with promising pharmacokinetic characteristics were identified. Overall, this study provides valuable insights into the QSAR of 1,2,4-Triazine-3(2H)-one derivative as potential anticancer agent, along with the design of new compounds and their assessment through molecular docking and dynamics simulations targeting the Tubulin-colchicine binding site. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=QSAR" title="QSAR">QSAR</a>, <a href="https://publications.waset.org/abstracts/search?q=molecular%20docking" title=" molecular docking"> molecular docking</a>, <a href="https://publications.waset.org/abstracts/search?q=ADMET" title=" ADMET"> ADMET</a>, <a href="https://publications.waset.org/abstracts/search?q=1" title=" 1"> 1</a>, <a href="https://publications.waset.org/abstracts/search?q=2" title="2">2</a>, <a href="https://publications.waset.org/abstracts/search?q=4-triazin-3%282H%29-ones" title="4-triazin-3(2H)-ones">4-triazin-3(2H)-ones</a>, <a href="https://publications.waset.org/abstracts/search?q=breast%20cancer" title=" breast cancer"> breast cancer</a>, <a href="https://publications.waset.org/abstracts/search?q=anticancer" title=" anticancer"> anticancer</a>, <a href="https://publications.waset.org/abstracts/search?q=molecular%20dynamic%20simulations" title=" molecular dynamic simulations"> molecular dynamic simulations</a>, <a href="https://publications.waset.org/abstracts/search?q=MMPBSA%20calculation" title=" MMPBSA calculation"> MMPBSA calculation</a> </p> <a href="https://publications.waset.org/abstracts/167402/exploring-124-triazine-32h-one-derivatives-as-anticancer-agents-for-breast-cancer-a-qsar-molecular-docking-admet-and-molecular-dynamics" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/167402.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">2163</span> Docking and Dynamic Molecular Study of Isoniazid Derivatives as Anti-Tuberculosis Drug Candidate</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Richa%20Mardianingrum">Richa Mardianingrum</a>, <a href="https://publications.waset.org/abstracts/search?q=Srie%20R.%20N.%20Endah"> Srie R. N. Endah</a> </p> <p class="card-text"><strong>Abstract:</strong></p> In this research, we have designed four isoniazid derivatives i.e., isonicotinohydrazide (1-isonicotinoyl semicarbazide, 1-thiosemi isonicotinoyl carbazide, N '-(1,3-dimethyl-1 h-pyrazole-5-carbonyl) isonicotino hydrazide, and N '-(1,2,3- 4-thiadiazole-carbonyl) isonicotinohydrazide. The docking and molecular dynamic have performed to them in order to study its interaction with Mycobacterium tuberculosis Enoyl-Acyl Carrier Protein Reductase (InhA). Based on this research, all of the compounds were predicted to have a stable interaction with Mycobacterium tuberculosis Enoyl-Acyl Carrier Protein Reductase (INHA) receptor, so they could be used as an anti-tuberculosis drug candidate. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=anti-tuberculosis" title="anti-tuberculosis">anti-tuberculosis</a>, <a href="https://publications.waset.org/abstracts/search?q=docking" title=" docking"> docking</a>, <a href="https://publications.waset.org/abstracts/search?q=Inhibin%20alpha%20subunit" title=" Inhibin alpha subunit"> Inhibin alpha subunit</a>, <a href="https://publications.waset.org/abstracts/search?q=InhA" title=" InhA"> InhA</a>, <a href="https://publications.waset.org/abstracts/search?q=inhibition" title=" inhibition"> inhibition</a>, <a href="https://publications.waset.org/abstracts/search?q=synthesis" title=" synthesis"> synthesis</a>, <a href="https://publications.waset.org/abstracts/search?q=isonicotinohydrazide" title=" isonicotinohydrazide"> isonicotinohydrazide</a> </p> <a href="https://publications.waset.org/abstracts/92270/docking-and-dynamic-molecular-study-of-isoniazid-derivatives-as-anti-tuberculosis-drug-candidate" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/92270.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">181</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">2162</span> Binding Studies of Complexes of Anticancer Drugs with DNA and Enzymes Involved in DNA Replication Using Molecular Docking and Cell Culture Techniques</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Fouzia%20Perveen">Fouzia Perveen</a>, <a href="https://publications.waset.org/abstracts/search?q=Rumana%20Qureshi"> Rumana Qureshi</a> </p> <p class="card-text"><strong>Abstract:</strong></p> The presently studied twelve anticancer drugs are the cytotoxic agents which inhibit the replication of DNA and activity of enzymes involved in DNA replication namely topoisomerase-II, polymerase and helicase and have shown remarkable anticancer activity in clinical trials. In this study, we performed molecular docking studies of twelve antitumor drugs against DNA and DNA enzymes in the presence and absence of ascorbic acid (AA) and developed the quantitative structure-activity relationship (QSAR) model for anticancer activity screening. A number of electronic and steric descriptors were calculated using MOE software package. QSAR was established showing a correlation of binding strength with various physicochemical descriptors. Out of these twelve, eight cytotoxic drugs were tested on Non-Small Cell Lung Cancer cell lines (H-157 and H-1299) in the absence and presence of ascorbic acid and experimental IC50 values were calculated. From the docking studies, binding constants were calculated indicating the strength of drug-DNA and drug-enzyme complex formation and it was correlated to the IC50 values (both experimental and theoretical). These results can offer useful references for directing the molecular design of DNA enzyme inhibitor with improved anticancer activity. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=ascorbic%20acid" title="ascorbic acid">ascorbic acid</a>, <a href="https://publications.waset.org/abstracts/search?q=binding%20constant" title=" binding constant"> binding constant</a>, <a href="https://publications.waset.org/abstracts/search?q=cytotoxic%20agents" title=" cytotoxic agents"> cytotoxic agents</a>, <a href="https://publications.waset.org/abstracts/search?q=cell%20culture" title=" cell culture"> cell culture</a>, <a href="https://publications.waset.org/abstracts/search?q=DNA" title=" DNA"> DNA</a>, <a href="https://publications.waset.org/abstracts/search?q=DNA%20enzymes" title=" DNA enzymes"> DNA enzymes</a>, <a href="https://publications.waset.org/abstracts/search?q=molecular%20docking" title=" molecular docking"> molecular docking</a> </p> <a href="https://publications.waset.org/abstracts/23535/binding-studies-of-complexes-of-anticancer-drugs-with-dna-and-enzymes-involved-in-dna-replication-using-molecular-docking-and-cell-culture-techniques" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/23535.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">427</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">2161</span> Contribution of Artificial Intelligence in the Studies of Natural Compounds Against SARS-COV-2</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Salah%20Belaidi">Salah Belaidi</a> </p> <p class="card-text"><strong>Abstract:</strong></p> We have carried out extensive and in-depth research to search for bioactive compounds based on Algerian plants. A selection of 50 ligands from Algerian medicinal plants. Several compounds used in herbal medicine have been drawn using Marvin Sketch software. We determined the three-dimensional structures of the ligands with the MMFF94 force field in order to prepare these ligands for molecular docking. The 3D protein structure of the SARS-CoV-2 main protease was taken from the Protein Data Bank. We used AutoDockVina software to apply molecular docking. The hydrogen atoms were added during the molecular docking process, and all the twist bonds of the ligands were added using the (ligand) module in the AutoDock software. The COVID-19 main protease (Mpro) is a key enzyme that plays a vital role in viral transcription and mediating replication, so it is a very attractive drug target for SARS-CoV-2. In this work, an evaluation was carried out on the biologically active compounds present in these selected medicinal plants as effective inhibitors of the protease enzyme of COVID-19, with an in-depth computational calculation of the molecular docking using the Autodock Vina software. The top 7 ligands: Phloroglucinol, Afzelin, Myricetin-3-O- rutinosidTricin 7-neohesperidoside, Silybin, Silychristinthat and Kaempferol are selected among the 50 molecules studied which are Algerian medicinal plants, whose selection is based on the best binding energy which is relatively low compared to the reference molecule with binding affinities of -9.3, -9.3, -9, -8.9, -8 .5, 8.3 and -8.3 kcal mol-1 respectively. Then, we analyzed the ADME properties of the best7 ligands using the web server SwissADME. Two ligands (Silybin, Silychristin) were found to be potential candidates for the discovery and design of novel drug inhibitors of the protease enzyme of SARS-CoV-2. The stability of the two ligands in complexing with the Mpro protease was validated by molecular dynamics simulation; they revealed a stable trajectory in both techniques, RMSD and RMSF, by showing molecular properties with coherent interactions in molecular dynamics simulations. Finally, we conclude that the Silybin ligand forms a more stable complex with the Mpro protease compared to the Silychristin ligand. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=COVID-19" title="COVID-19">COVID-19</a>, <a href="https://publications.waset.org/abstracts/search?q=medicinal%20plants" title=" medicinal plants"> medicinal plants</a>, <a href="https://publications.waset.org/abstracts/search?q=molecular%20docking" title=" molecular docking"> molecular docking</a>, <a href="https://publications.waset.org/abstracts/search?q=ADME%20properties" title=" ADME properties"> ADME properties</a>, <a href="https://publications.waset.org/abstracts/search?q=molecular%20dynamics" title=" molecular dynamics"> molecular dynamics</a> </p> <a href="https://publications.waset.org/abstracts/188747/contribution-of-artificial-intelligence-in-the-studies-of-natural-compounds-against-sars-cov-2" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/188747.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">35</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">2160</span> In Silico Study of Antiviral Drugs Against Three Important Proteins of Sars-Cov-2 Using Molecular Docking Method</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Alireza%20Jalalvand">Alireza Jalalvand</a>, <a href="https://publications.waset.org/abstracts/search?q=Maryam%20Saleh"> Maryam Saleh</a>, <a href="https://publications.waset.org/abstracts/search?q=Somayeh%20Behjat%20Khatouni"> Somayeh Behjat Khatouni</a>, <a href="https://publications.waset.org/abstracts/search?q=Zahra%20Bahri%20Najafi"> Zahra Bahri Najafi</a>, <a href="https://publications.waset.org/abstracts/search?q=Foroozan%20Fatahinia"> Foroozan Fatahinia</a>, <a href="https://publications.waset.org/abstracts/search?q=Narges%20Ismailzadeh"> Narges Ismailzadeh</a>, <a href="https://publications.waset.org/abstracts/search?q=Behrokh%20Farahmand"> Behrokh Farahmand</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Object: In the last two decades, the recent outbreak of Coronavirus (SARS-CoV-2) imposed a global pandemic in the world. Despite the increasing prevalence of the disease, there are no effective drugs to treat it. A suitable and rapid way to afford an effective drug and treat the global pandemic is a computational drug study. This study used molecular docking methods to examine the potential inhibition of over 50 antiviral drugs against three fundamental proteins of SARS-CoV-2. METHODS: Through a literature review, three important proteins (a key protease, RNA-dependent RNA polymerase (RdRp), and spike) were selected as drug targets. Three-dimensional (3D) structures of protease, spike, and RdRP proteins were obtained from the Protein Data Bank. Protein had minimal energy. Over 50 antiviral drugs were considered candidates for protein inhibition and their 3D structures were obtained from drug banks. The Autodock 4.2 software was used to define the molecular docking settings and run the algorithm. RESULTS: Five drugs, including indinavir, lopinavir, saquinavir, nelfinavir, and remdesivir, exhibited the highest inhibitory potency against all three proteins based on the binding energies and drug binding positions deduced from docking and hydrogen-bonding analysis. Conclusions: According to the results, among the drugs mentioned, saquinavir and lopinavir showed the highest inhibitory potency against all three proteins compared to other drugs. It may enter laboratory phase studies as a dual-drug treatment to inhibit SARS-CoV-2. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=covid-19" title="covid-19">covid-19</a>, <a href="https://publications.waset.org/abstracts/search?q=drug%20repositioning" title=" drug repositioning"> drug repositioning</a>, <a href="https://publications.waset.org/abstracts/search?q=molecular%20docking" title=" molecular docking"> molecular docking</a>, <a href="https://publications.waset.org/abstracts/search?q=lopinavir" title=" lopinavir"> lopinavir</a>, <a href="https://publications.waset.org/abstracts/search?q=saquinavir" title=" saquinavir"> saquinavir</a> </p> <a href="https://publications.waset.org/abstracts/165518/in-silico-study-of-antiviral-drugs-against-three-important-proteins-of-sars-cov-2-using-molecular-docking-method" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/165518.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">88</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">2159</span> 2-Thioimidazole Analogues: Synthesis, in silico Studies and in vitro Anticancer and Antiprotozoal Evaluation</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Drashti%20G.%20Daraji">Drashti G. Daraji</a>, <a href="https://publications.waset.org/abstracts/search?q=Rosa%20E.%20Moo-Puc"> Rosa E. Moo-Puc</a>, <a href="https://publications.waset.org/abstracts/search?q=Hitesh%20D.%20Patel"> Hitesh D. Patel</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Substituted 2-Thioimidazole analogues have been synthesized and confirmed by advanced spectroscopic techniques. Among them, ten compounds have been selected and evaluated for their in vitro anti-cancer activity at the National Cancer Institute (NCI) for testing against a panel of 60 different human tumor cell lines derived from nine neoplastic cancer types. Furthermore, synthesized compounds were tested for their in vitro antiprotozoal activity, and none of them exhibited significant potency against antiprotozoans. It was observed that the tested all compounds seem effective on the UACC-62 melanoma cancer cell line as compared to other cancer cell lines and also exhibited the least potent in the Non-Small Cell Lung Cancer cell line in one-dose screening. In silico studies of these derivatives were carried out by molecular docking techniques and Absorption, Distribution, Metabolism, and Excretion (ADME) using Schrödinger software to find potent B-Raf kinase inhibitor (PDB ID: 3OG7). All the compounds have been performed for docking study; Compound D4 has a good docking score for melanoma cancer as compared with other. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=anticancer%20activity" title="anticancer activity">anticancer activity</a>, <a href="https://publications.waset.org/abstracts/search?q=cancer%20cell%20line" title=" cancer cell line"> cancer cell line</a>, <a href="https://publications.waset.org/abstracts/search?q=2-thio%20imidazole" title=" 2-thio imidazole"> 2-thio imidazole</a>, <a href="https://publications.waset.org/abstracts/search?q=one-dose%20assay" title=" one-dose assay"> one-dose assay</a>, <a href="https://publications.waset.org/abstracts/search?q=molecular%20docking" title=" molecular docking"> molecular docking</a> </p> <a href="https://publications.waset.org/abstracts/112257/2-thioimidazole-analogues-synthesis-in-silico-studies-and-in-vitro-anticancer-and-antiprotozoal-evaluation" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/112257.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">143</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">2158</span> Experimental and Theoretical Approach, Hirshfeld Surface, Reduced Density Gradient, Molecular Docking of a Thiourea Derivative</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Noureddine%20Benharkat">Noureddine Benharkat</a>, <a href="https://publications.waset.org/abstracts/search?q=Abdelkader%20Chouaih"> Abdelkader Chouaih</a>, <a href="https://publications.waset.org/abstracts/search?q=Nourdine%20Boukabcha"> Nourdine Boukabcha</a> </p> <p class="card-text"><strong>Abstract:</strong></p> A thiourea derivative compound was synthesized and subjected to structural analysis using single-crystal X-ray diffraction (XRD). The crystallographic data unveiled its crystallization in the P21/c space group within the monoclinic system. Examination of the dihedral angles indicated a notable non-planar structure. To support and interpret these resulats, density functional theory (DFT) calculations were conducted utilizing the B3LYP functional along with a 6–311 G (d, p) basis set. Additionally, to assess the contribution of intermolecular interactions, Hirshfeld surface analysis and 2D fingerprint plots were employed. Various types of interactions, whether weak intramolecular or intermolecular, within a molecule can significantly impact its stability. The distinctive signature of non-covalent interactions can be detected solely through electron density analysis. The NCI-RDG analysis was employed to investigate both repulsive and attractive van der Waals interactions while also calculating the energies associated with intermolecular interactions and their characteristics. Additionally, a molecular docking study was studied to explain the structure-activity relationship, revealing that the title compound exhibited an affinity energy of -6.8 kcal/mol when docked with B-DNA (1BNA). <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=computational%20chemistry" title="computational chemistry">computational chemistry</a>, <a href="https://publications.waset.org/abstracts/search?q=density%20functional%20theory" title=" density functional theory"> density functional theory</a>, <a href="https://publications.waset.org/abstracts/search?q=crystallography" title=" crystallography"> crystallography</a>, <a href="https://publications.waset.org/abstracts/search?q=molecular%20docking" title=" molecular docking"> molecular docking</a>, <a href="https://publications.waset.org/abstracts/search?q=molecular%20structure" title=" molecular structure"> molecular structure</a>, <a href="https://publications.waset.org/abstracts/search?q=powder%20x-ray%20diffraction" title=" powder x-ray diffraction"> powder x-ray diffraction</a>, <a href="https://publications.waset.org/abstracts/search?q=single%20crystal%20x-ray%20diffraction" title=" single crystal x-ray diffraction"> single crystal x-ray diffraction</a> </p> <a href="https://publications.waset.org/abstracts/184452/experimental-and-theoretical-approach-hirshfeld-surface-reduced-density-gradient-molecular-docking-of-a-thiourea-derivative" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/184452.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">60</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">2157</span> Synthesis, Inhibitory Activity, and Molecular Modelling of 2-Hydroxy-3-Oxo-3-Phenylpropionate Derivatives as HIV-1-Integrase Inhibitors</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=O.%20J.%20Jesumoroti">O. J. Jesumoroti</a>, <a href="https://publications.waset.org/abstracts/search?q=Faridoon"> Faridoon</a>, <a href="https://publications.waset.org/abstracts/search?q=R.%20Klein"> R. Klein</a>, <a href="https://publications.waset.org/abstracts/search?q=K.%20A.%20Iobb"> K. A. Iobb</a>, <a href="https://publications.waset.org/abstracts/search?q=D.%20Mnkadhla"> D. Mnkadhla</a>, <a href="https://publications.waset.org/abstracts/search?q=H.%20C.%20Hoppe"> H. C. Hoppe</a>, <a href="https://publications.waset.org/abstracts/search?q=P.%20T.%20Kaye"> P. T. Kaye </a> </p> <p class="card-text"><strong>Abstract:</strong></p> The 1, 3-aryl diketo acids (DKA) based agents represent an important class of HIV integrase (IN) strand transfer inhibitors. In other to study the chelating role of the divalent metal ion in the inhibition of IN strand transfer, we designed and synthesized a series of 2-hydroxy-3-oxo-3-phenyl propionate derivatives with the notion that such compounds could interact with the divalent ion in the active site of IN. The synthetic sequence to the desired compounds involves the concept of Doebner knoevenagel condensation, Fischer esterification and ketohydroxylation using neuclophilic re-oxidant; compounds were characterized by their IR, IHNMR, 13CNMR, HRMS spectroscopic data and melting point determination. Also, molecular docking was employed in this study and it was revealed that there is interaction with the active site of the enzyme. However, there is disparity in the corresponding anti-HIV activity determined by the experimental bioassay. These compounds lack potency at low micromolar concentration when compared to the results of the docking studies. Nevertheless, the results of the study suggest modification of the aryl ring with one or two hydroxyl groups to improve the inhibitory activity. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=anti-HIV-1%20integrase" title="anti-HIV-1 integrase">anti-HIV-1 integrase</a>, <a href="https://publications.waset.org/abstracts/search?q=ketohydroxylation" title=" ketohydroxylation"> ketohydroxylation</a>, <a href="https://publications.waset.org/abstracts/search?q=molecular%20docking" title=" molecular docking"> molecular docking</a>, <a href="https://publications.waset.org/abstracts/search?q=propionate%20derivatives" title=" propionate derivatives "> propionate derivatives </a> </p> <a href="https://publications.waset.org/abstracts/44981/synthesis-inhibitory-activity-and-molecular-modelling-of-2-hydroxy-3-oxo-3-phenylpropionate-derivatives-as-hiv-1-integrase-inhibitors" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/44981.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">2156</span> Synthesis, Characterization, and Biological Evaluation of 1,3,4-Mercaptooxadiazole Ether Derivatives Analogs as Antioxidant, Cytotoxic, and Molecular Docking Studies</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Desta%20Gebretekle%20Shiferaw">Desta Gebretekle Shiferaw</a>, <a href="https://publications.waset.org/abstracts/search?q=Balakrishna%20Kalluraya"> Balakrishna Kalluraya</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Oxadiazoles and their derivatives with thioether functionalities represent a new and exciting class of physiologically active heterocyclic compounds. Several molecules with these moieties play a vital role in pharmaceuticals because of their diverse biological activities. This paper describes a new class of 1,3,4- oxadiazole-2-thioethers with acetophenone, coumarin, and N-phenyl acetamide residues (S-alkylation), with the hope that the addition of various biologically active molecules will have a synergistic effect on anticancer activity. The structure of the synthesized title compounds was determined by the combined methods of IR, proton-NMR, carbon-13-NMR, and mass spectrometry. Further, all the newly prepared molecules were assessed against their antioxidant activity. Furthermore, four compounds were assessed for their molecular docking interactions and cytotoxicity activity. The synthesized derivatives have shown moderate antioxidant activity compared to the standard BHA. The IC50 of the tilted molecules (11b, 11c, 13b, and 14b) observed for in vitro anti-cancer activities were 11.20, 15.73, 59.61, and 27.66 g/ml at 72-hour treatment time against the A549 cell lines, respectively. The tested compounds' biological evaluation showed that 11b is the most effective molecule in the series. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=antioxidant%20activity" title="antioxidant activity">antioxidant activity</a>, <a href="https://publications.waset.org/abstracts/search?q=cytotoxicity%20activity" title=" cytotoxicity activity"> cytotoxicity activity</a>, <a href="https://publications.waset.org/abstracts/search?q=molecular%20docking" title=" molecular docking"> molecular docking</a>, <a href="https://publications.waset.org/abstracts/search?q=1" title=" 1"> 1</a>, <a href="https://publications.waset.org/abstracts/search?q=3" title=" 3"> 3</a>, <a href="https://publications.waset.org/abstracts/search?q=4-Oxadiazole-2%20thioether%20derivatives" title=" 4-Oxadiazole-2 thioether derivatives"> 4-Oxadiazole-2 thioether derivatives</a> </p> <a href="https://publications.waset.org/abstracts/160395/synthesis-characterization-and-biological-evaluation-of-134-mercaptooxadiazole-ether-derivatives-analogs-as-antioxidant-cytotoxic-and-molecular-docking-studies" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/160395.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">90</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">2155</span> In-Silico Investigation of Phytochemicals from Ocimum Sanctum as Plausible Antiviral Agent in COVID-19</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Dileep%20Kumar">Dileep Kumar</a>, <a href="https://publications.waset.org/abstracts/search?q=Janhavi%20Ramchandra%20Rao%20Kumar"> Janhavi Ramchandra Rao Kumar</a>, <a href="https://publications.waset.org/abstracts/search?q=Rao"> Rao</a> </p> <p class="card-text"><strong>Abstract:</strong></p> COVID-19 has ravaged the globe, and it is spreading its Spectre day by day. In the absence of established drugs, this disease has created havoc. Some of the infected persons are symptomatic or asymptomatic. The respiratory system, cardiac system, digestive system, etc. in human beings are affected by this virus. In our present investigation, we have undertaken a study of the Indian Ayurvedic herb, Ocimum sanctum against SARS-CoV-2 using molecular docking and dynamics studies. The docking analysis was performed on the Glide module of Schrödinger suite on two different proteins from SARS-CoV-2 viz. NSP15 Endoribonuclease and spike receptor-binding domain. MM-GBSA based binding free energy calculations also suggest the most favorable binding affinities of carvacrol, β elemene, and β caryophyllene with binding energies of −61.61, 58.23, and −54.19 Kcal/mol respectively with spike receptor-binding domain and NSP15 Endoribonuclease. It rekindles our hope for the design and development of new drug candidates for the treatment of COVID19. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=molecular%20docking" title="molecular docking">molecular docking</a>, <a href="https://publications.waset.org/abstracts/search?q=COVID-19" title=" COVID-19"> COVID-19</a>, <a href="https://publications.waset.org/abstracts/search?q=ocimum%20sanctum" title=" ocimum sanctum"> ocimum sanctum</a>, <a href="https://publications.waset.org/abstracts/search?q=binding%20energy" title=" binding energy"> binding energy</a> </p> <a href="https://publications.waset.org/abstracts/130061/in-silico-investigation-of-phytochemicals-from-ocimum-sanctum-as-plausible-antiviral-agent-in-covid-19" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/130061.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">187</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">2154</span> Synthesis, Molecular Docking, and Cytotoxic Activity of Novel Triazolopyridazine Derivatives </h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Azza%20T.%20Tahera">Azza T. Tahera</a>, <a href="https://publications.waset.org/abstracts/search?q=Eman%20M.%20Ahmeda"> Eman M. Ahmeda</a>, <a href="https://publications.waset.org/abstracts/search?q=Nadia%20A.%20Khalila"> Nadia A. Khalila</a>, <a href="https://publications.waset.org/abstracts/search?q=Yassin%20M.%20Nissanb"> Yassin M. Nissanb</a> </p> <p class="card-text"><strong>Abstract:</strong></p> New 3-(pyridin-4-yl)-[1,2,4] triazolo [4,3-b] pyridazine derivatives 2a-i, 4a,b and 6a,b were designed, synthesized and evaluated as cytotoxic agents. All compounds were investigated for their in vitro cytotoxicity at a single dose 10-5M concentration towards 60 cancer cell lines according to USA NCI protocol. The preliminary screening results showed that the majority of tested compounds exhibited remarkable activity against SR (leukemia) cell panel. Molecular docking for all synthesized compounds was performed on the active site of c-Met kinase. The most active compounds, 2f and 4a were further evaluated at a seven dose level screening and their IC50 as a c-Met kinase inhibitors were determined in vitro. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=triazolopyridazines" title="triazolopyridazines">triazolopyridazines</a>, <a href="https://publications.waset.org/abstracts/search?q=pyridazines" title=" pyridazines"> pyridazines</a>, <a href="https://publications.waset.org/abstracts/search?q=cytotoxic%20activity" title=" cytotoxic activity"> cytotoxic activity</a>, <a href="https://publications.waset.org/abstracts/search?q=cell%20panel" title=" cell panel"> cell panel</a> </p> <a href="https://publications.waset.org/abstracts/22560/synthesis-molecular-docking-and-cytotoxic-activity-of-novel-triazolopyridazine-derivatives" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/22560.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">537</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">2153</span> Investigations on the Cytotoxicity and Antimicrobial Activities of Terezine E and 14-Hydroxyterezine D</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Mariam%20Mojally">Mariam Mojally</a>, <a href="https://publications.waset.org/abstracts/search?q=Randa%20Abdou"> Randa Abdou</a>, <a href="https://publications.waset.org/abstracts/search?q=Wisal%20Bokhari"> Wisal Bokhari</a>, <a href="https://publications.waset.org/abstracts/search?q=Sultan%20Sab"> Sultan Sab</a>, <a href="https://publications.waset.org/abstracts/search?q=Mohammed%20Dawoud"> Mohammed Dawoud</a>, <a href="https://publications.waset.org/abstracts/search?q=Amjad%20Albohy"> Amjad Albohy</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Secondary metabolites produced by endophytes are an excellent source of biologically active compounds. In our current study, we evaluated terezine E and 14-hydroxyterezine D for binding to the active site of histone deacetylase (PDB ID: 4CBT) and matrix metalloproteinase 9 (PDB ID: 4H3X) by molecular docking using AutoDock Vina software after having tested their cytotoxic activities on three cell lines (human ductal breast epithelial tumor cells (T47D)-HCC1937), human hepatocarcinoma cell line (HepG2)-HB8065), and human colorectal carcinoma cells (HCT-116)-TCP1006, purchased from ATCC, USA)). Additionally, their antimicrobial activities were investigated, and their minimum inhibitory concentration (MIC) values were determined against P. notatum and S. aureus by the broth microdilution method. Higher cytotoxicity was observed for terezine E against all tested cell lines compared to 14-hydroxyterezine D. Molecular docking results supported the high cytotoxicity of terezine E and showed higher binding affinity with 4CBT with an energy score of 9 kcal/mol. Terezine E showed higher antibacterial and antifungal activities than 14-hydroxyrerezine D: MIC values were 15.45 and 21.73 mg/mL against S. aureus and 8.61 and 11.54 mg/mL against P. notatum, respectively <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=Terezine%20E" title="Terezine E">Terezine E</a>, <a href="https://publications.waset.org/abstracts/search?q=14-Hydroxyterezine%20D" title=" 14-Hydroxyterezine D"> 14-Hydroxyterezine D</a>, <a href="https://publications.waset.org/abstracts/search?q=cytotoxicity" title=" cytotoxicity"> cytotoxicity</a>, <a href="https://publications.waset.org/abstracts/search?q=antimicrobial%20activity" title=" antimicrobial activity"> antimicrobial activity</a>, <a href="https://publications.waset.org/abstracts/search?q=molecular%20docking" title=" molecular docking"> molecular docking</a> </p> <a href="https://publications.waset.org/abstracts/179873/investigations-on-the-cytotoxicity-and-antimicrobial-activities-of-terezine-e-and-14-hydroxyterezine-d" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/179873.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">73</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">2152</span> Cannabis Sativa L as Natural Source of Promising Anti-Alzheimer Drug Candidates: A Comprehensive Computational Approach Including Molecular Docking, Molecular Dynamics, ADMET and MM-PBSA Studies</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Hassan%20Nour">Hassan Nour</a>, <a href="https://publications.waset.org/abstracts/search?q=Nouh%20Mounadi"> Nouh Mounadi</a>, <a href="https://publications.waset.org/abstracts/search?q=Oussama%20Abchir"> Oussama Abchir</a>, <a href="https://publications.waset.org/abstracts/search?q=Belaidi%20Salah"> Belaidi Salah</a>, <a href="https://publications.waset.org/abstracts/search?q=Samir%20Chtita"> Samir Chtita</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Cholinesterase enzymes are biological catalysts essential for the transformation of acetylcholine, which is a neurotransmitter implicated in memory and learning, into acetic acid and choline, altering the neurotransmission process in Alzheimer’s disease patients. Therefore, inhibition of cholinesterase enzymes is a relevant strategy for the symptomatic treatment of Alzheimer’s disease. The current investigation aims to explore potential cholinesterase (ChE) inhibitors through a comprehensive computational approach. Forty-nine phytoconstituents extracted from Cannabis sativa L. were in-silico screened using molecular docking and pharmacokinetic and toxicological analysis to evaluate their possible inhibitory effect on the cholinesterase enzymes. Two phytoconstituents belonging to cannabinoid derivatives were revealed to be promising candidates for Alzheimer's therapy by acting as cholinesterase inhibitors. They have exhibited high binding affinities towards the cholinesterase enzymes and showed their ability to interact with key residues involved in cholinesterase enzymatic activity. In addition, they presented good ADMET profiles allowing them to be promising oral drug candidates. Furthermore, molecular dynamics (MD) simulations were executed to explore their interaction stability under mimetic biological conditions and thus support our findings. To corroborate the docking results, the binding free energy corresponding to the more stable ligand-ChE complexes was re-estimated by applying the MM-PBSA method. MD and MM-PBSA studies affirmed that the ligand-ChE recognition is a spontaneous reaction leading to stable complexes. The conducted investigations have led to great findings that would strongly guide the pharmaceutical industries toward the rational development of potent anti-Alzheimer agents. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=Alzheimer%E2%80%99s%20disease" title="Alzheimer’s disease">Alzheimer’s disease</a>, <a href="https://publications.waset.org/abstracts/search?q=molecular%20docking" title=" molecular docking"> molecular docking</a>, <a href="https://publications.waset.org/abstracts/search?q=Cannabis%20sativa%20L." title=" Cannabis sativa L."> Cannabis sativa L.</a>, <a href="https://publications.waset.org/abstracts/search?q=cholinesterase%20inhibitors" title=" cholinesterase inhibitors"> cholinesterase inhibitors</a>, <a href="https://publications.waset.org/abstracts/search?q=molecular%20dynamics" title=" molecular dynamics"> molecular dynamics</a>, <a href="https://publications.waset.org/abstracts/search?q=ADMET" title=" ADMET"> ADMET</a>, <a href="https://publications.waset.org/abstracts/search?q=MM-PBSA" title=" MM-PBSA"> MM-PBSA</a> </p> <a href="https://publications.waset.org/abstracts/171128/cannabis-sativa-l-as-natural-source-of-promising-anti-alzheimer-drug-candidates-a-comprehensive-computational-approach-including-molecular-docking-molecular-dynamics-admet-and-mm-pbsa-studies" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/171128.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">83</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">2151</span> Molecular Interactions Driving RNA Binding to hnRNPA1 Implicated in Neurodegeneration</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Sakina%20Fatima">Sakina Fatima</a>, <a href="https://publications.waset.org/abstracts/search?q=Joseph-Patrick%20W.%20E.%20Clarke"> Joseph-Patrick W. E. Clarke</a>, <a href="https://publications.waset.org/abstracts/search?q=Patricia%20A.%20Thibault"> Patricia A. Thibault</a>, <a href="https://publications.waset.org/abstracts/search?q=Subha%20Kalyaanamoorthy"> Subha Kalyaanamoorthy</a>, <a href="https://publications.waset.org/abstracts/search?q=Michael%20Levin"> Michael Levin</a>, <a href="https://publications.waset.org/abstracts/search?q=Aravindhan%20Ganesan"> Aravindhan Ganesan</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Heteronuclear ribonucleoprotein (hnRNPA1 or A1) is associated with the pathology of different diseases, including neurological disorders and cancers. In particular, the aggregation and dysfunction of A1 have been identified as a critical driver for neurodegeneration (NDG) in Multiple Sclerosis (MS). Structurally, A1 includes a low-complexity domain (LCD) and two RNA-recognition motifs (RRMs), and their interdomain coordination may play a crucial role in A1 aggregation. Previous studies propose that RNA-inhibitors or nucleoside analogs that bind to RRMs can potentially prevent A1 self-association. Therefore, molecular-level understanding of the structures, dynamics, and nucleotide interactions with A1 RRMs can be useful for developing therapeutics for NDG in MS. In this work, a combination of computational modelling and biochemical experiments were employed to analyze a set of RNA-A1 RRM complexes. Initially, the atomistic models of RNA-RRM complexes were constructed by modifying known crystal structures (e.g., PDBs: 4YOE and 5MPG), and through molecular docking calculations. The complexes were optimized using molecular dynamics simulations (200-400 ns), and their binding free energies were computed. The binding affinities of the selected complexes were validated using a thermal shift assay. Further, the most important molecular interactions that contributed to the overall stability of the RNA-A1 RRM complexes were deduced. The results highlight that adenine and guanine are the most suitable nucleotides for high-affinity binding with A1. These insights will be useful in the rational design of nucleotide-analogs for targeting A1 RRMs. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=hnRNPA1" title="hnRNPA1">hnRNPA1</a>, <a href="https://publications.waset.org/abstracts/search?q=molecular%20docking" title=" molecular docking"> molecular docking</a>, <a href="https://publications.waset.org/abstracts/search?q=molecular%20dynamics" title=" molecular dynamics"> molecular dynamics</a>, <a href="https://publications.waset.org/abstracts/search?q=RNA-binding%20proteins" title=" RNA-binding proteins"> RNA-binding proteins</a> </p> <a href="https://publications.waset.org/abstracts/155246/molecular-interactions-driving-rna-binding-to-hnrnpa1-implicated-in-neurodegeneration" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/155246.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">119</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">2150</span> An Inverse Docking Approach for Identifying New Potential Anticancer Targets</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Soujanya%20Pasumarthi">Soujanya Pasumarthi</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Inverse docking is a relatively new technique that has been used to identify potential receptor targets of small molecules. Our docking software package MDock is well suited for such an application as it is both computationally efficient, yet simultaneously shows adequate results in binding affinity predictions and enrichment tests. As a validation study, we present the first stage results of an inverse-docking study which seeks to identify potential direct targets of PRIMA-1. PRIMA-1 is well known for its ability to restore mutant p53's tumor suppressor function, leading to apoptosis in several types of cancer cells. For this reason, we believe that potential direct targets of PRIMA-1 identified in silico should be experimentally screened for their ability to inhibitcancer cell growth. The highest-ranked human protein of our PRIMA-1 docking results is oxidosqualene cyclase (OSC), which is part of the cholesterol synthetic pathway. The results of two followup experiments which treat OSC as a possible anti-cancer target are promising. We show that both PRIMA-1 and Ro 48-8071, a known potent OSC inhibitor, significantly reduce theviability of BT-474 breast cancer cells relative to normal mammary cells. In addition, like PRIMA-1, we find that Ro 48-8071 results in increased binding of mutant p53 to DNA in BT- 474cells (which highly express p53). For the first time, Ro 48-8071 is shown as a potent agent in killing human breast cancer cells. The potential of OSC as a new target for developing anticancer therapies is worth further investigation. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=inverse%20docking" title="inverse docking">inverse docking</a>, <a href="https://publications.waset.org/abstracts/search?q=in%20silico%20screening" title=" in silico screening"> in silico screening</a>, <a href="https://publications.waset.org/abstracts/search?q=protein-ligand%20interactions" title=" protein-ligand interactions"> protein-ligand interactions</a>, <a href="https://publications.waset.org/abstracts/search?q=molecular%20docking" title=" molecular docking "> molecular docking </a> </p> <a href="https://publications.waset.org/abstracts/9217/an-inverse-docking-approach-for-identifying-new-potential-anticancer-targets" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/9217.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">446</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">2149</span> Towards Designing of a Potential New HIV-1 Protease Inhibitor Using Quantitative Structure-Activity Relationship Study in Combination with Molecular Docking and Molecular Dynamics Simulations</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Mouna%20Baassi">Mouna Baassi</a>, <a href="https://publications.waset.org/abstracts/search?q=Mohamed%20Moussaoui"> Mohamed Moussaoui</a>, <a href="https://publications.waset.org/abstracts/search?q=Hatim%20Soufi"> Hatim Soufi</a>, <a href="https://publications.waset.org/abstracts/search?q=Sanchaita%20RajkhowaI"> Sanchaita RajkhowaI</a>, <a href="https://publications.waset.org/abstracts/search?q=Ashwani%20Sharma"> Ashwani Sharma</a>, <a href="https://publications.waset.org/abstracts/search?q=Subrata%20Sinha"> Subrata Sinha</a>, <a href="https://publications.waset.org/abstracts/search?q=Said%20Belaaouad"> Said Belaaouad</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Human Immunodeficiency Virus type 1 protease (HIV-1 PR) is one of the most challenging targets of antiretroviral therapy used in the treatment of AIDS-infected people. The performance of protease inhibitors (PIs) is limited by the development of protease mutations that can promote resistance to the treatment. The current study was carried out using statistics and bioinformatics tools. A series of thirty-three compounds with known enzymatic inhibitory activities against HIV-1 protease was used in this paper to build a mathematical model relating the structure to the biological activity. These compounds were designed by software; their descriptors were computed using various tools, such as Gaussian, Chem3D, ChemSketch and MarvinSketch. Computational methods generated the best model based on its statistical parameters. The model’s applicability domain (AD) was elaborated. Furthermore, one compound has been proposed as efficient against HIV-1 protease with comparable biological activity to the existing ones; this drug candidate was evaluated using ADMET properties and Lipinski’s rule. Molecular Docking performed on Wild Type and Mutant Type HIV-1 proteases allowed the investigation of the interaction types displayed between the proteases and the ligands, Darunavir (DRV) and the new drug (ND). Molecular dynamics simulation was also used in order to investigate the complexes’ stability, allowing a comparative study of the performance of both ligands (DRV & ND). Our study suggested that the new molecule showed comparable results to that of Darunavir and may be used for further experimental studies. Our study may also be used as a pipeline to search and design new potential inhibitors of HIV-1 proteases. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=QSAR" title="QSAR">QSAR</a>, <a href="https://publications.waset.org/abstracts/search?q=ADMET%20properties" title=" ADMET properties"> ADMET properties</a>, <a href="https://publications.waset.org/abstracts/search?q=molecular%20docking" title=" molecular docking"> molecular docking</a>, <a href="https://publications.waset.org/abstracts/search?q=molecular%20dynamics%20simulation." title=" molecular dynamics simulation."> molecular dynamics simulation.</a> </p> <a href="https://publications.waset.org/abstracts/187453/towards-designing-of-a-potential-new-hiv-1-protease-inhibitor-using-quantitative-structure-activity-relationship-study-in-combination-with-molecular-docking-and-molecular-dynamics-simulations" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/187453.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">39</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">2148</span> Cannabis Sativa L as Natural Source of Promising Anti-Alzheimer Drug Candidates: A Comprehensive Computational Approach Including Molecular Docking, Molecular Dynamics, Admet and MM-PBSA Studies</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Hassan%20Nour">Hassan Nour</a>, <a href="https://publications.waset.org/abstracts/search?q=Nouh%20Mounadi"> Nouh Mounadi</a>, <a href="https://publications.waset.org/abstracts/search?q=Oussama%20Abchir"> Oussama Abchir</a>, <a href="https://publications.waset.org/abstracts/search?q=Belaidi%20Salah"> Belaidi Salah</a>, <a href="https://publications.waset.org/abstracts/search?q=Samir%20Chtita"> Samir Chtita</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Cholinesterase enzymes are biological catalysts essential for the transformation of acetylcholine, which is a neurotransmitter implicated in memory and learning, into acetic acid and choline, altering the neurotransmission process in Alzheimer’s disease patients. Therefore, inhibition of cholinesterase enzymes is a relevant strategy for the symptomatic treatment of Alzheimer’s disease. The current investigation aims to explore potential Cholinesterase (ChE) inhibitors through a comprehensive computational approach. Forty-nine phytoconstituents extracted from Cannabis sativa L were in-silico screened using molecular docking, pharmacokinetic and toxicological analysis to evaluate their possible inhibitory effect towards the cholinesterase enzymes. Two phytoconstituents belonging to cannabinoid derivatives were revealed to be promising candidates for Alzheimer therapy by acting as cholinesterase inhibitors. They have exhibited high binding affinities towards the cholinesterase enzymes and showed their ability to interact with key residues involved in cholinesterase enzymatic activity. In addition, they presented good ADMET profiles allowing them to be promising oral drug candidates. Furthermore, molecular dynamics (MD) simulations were executed to explore their interactions stability under mimetic biological conditions and thus support our findings. To corroborate the docking results, the binding free energy corresponding to the more stable ligand-ChE complexes was re-estimated by applying the MM-PBSA method. MD and MM-PBSA studies affirmed that the ligand-ChE recognition is spontaneous reaction leading to stable complexes. The conducted investigations have led to great findings that would strongly guide the pharmaceutical industries towards the rational development of potent anti-Alzheimer agents. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=alzheimer%E2%80%99s%20disease" title="alzheimer’s disease">alzheimer’s disease</a>, <a href="https://publications.waset.org/abstracts/search?q=molecular%20docking" title=" molecular docking"> molecular docking</a>, <a href="https://publications.waset.org/abstracts/search?q=cannabis%20sativa%20l" title=" cannabis sativa l"> cannabis sativa l</a>, <a href="https://publications.waset.org/abstracts/search?q=cholinesterase%20inhibitors" title=" cholinesterase inhibitors"> cholinesterase inhibitors</a> </p> <a href="https://publications.waset.org/abstracts/171130/cannabis-sativa-l-as-natural-source-of-promising-anti-alzheimer-drug-candidates-a-comprehensive-computational-approach-including-molecular-docking-molecular-dynamics-admet-and-mm-pbsa-studies" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/171130.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">73</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">2147</span> Cholinesterase Inhibitory Indole Alkaloids from the Bark of Rauvolfia reflexa</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Mehran%20Fadaeinasab">Mehran Fadaeinasab</a>, <a href="https://publications.waset.org/abstracts/search?q=Alireza%20Basiri"> Alireza Basiri</a>, <a href="https://publications.waset.org/abstracts/search?q=Yalda%20Kia"> Yalda Kia</a>, <a href="https://publications.waset.org/abstracts/search?q=Hamed%20Karimian"> Hamed Karimian</a>, <a href="https://publications.waset.org/abstracts/search?q=Hapipah%20Mohd%20Ali"> Hapipah Mohd Ali</a>, <a href="https://publications.waset.org/abstracts/search?q=Vikneswaran%20Murugaiyah"> Vikneswaran Murugaiyah</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Two new, rauvolfine C and 3- methyl-10,11-dimethoxyl-6- methoxycarbonyl- β- carboline, along with five known indole alkaloids, macusine B, vinorine, undulifoline, isoresrpiline and rescinnamine were isolated from the bark of Rauvolfia reflexa. All the compounds showed good to moderate cholinesterase inhibitory activity with IC50 values in the range of 8.06 to 73.23 πM, except rauvolfine C that was inactive against acetylcholinesterase (AChE). Rescinnamine, a dual inhibitor was found to be the most potent inhibitor among the isolated alkaloids against both AChE and butyrylcholinesterase (BChE). Molecular docking revealed that rescinnamine interacted differently on AChE and BChE, by means of hydrophobic interactions and hydrogen bonding. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=Rauvolfia%20reflexa" title="Rauvolfia reflexa">Rauvolfia reflexa</a>, <a href="https://publications.waset.org/abstracts/search?q=indole%20alkaloids" title=" indole alkaloids"> indole alkaloids</a>, <a href="https://publications.waset.org/abstracts/search?q=acetylcholinesterase" title=" acetylcholinesterase"> acetylcholinesterase</a>, <a href="https://publications.waset.org/abstracts/search?q=butyrylcholinesterase" title=" butyrylcholinesterase"> butyrylcholinesterase</a>, <a href="https://publications.waset.org/abstracts/search?q=molecular%20docking" title=" molecular docking"> molecular docking</a> </p> <a href="https://publications.waset.org/abstracts/30034/cholinesterase-inhibitory-indole-alkaloids-from-the-bark-of-rauvolfia-reflexa" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/30034.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">592</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">2146</span> Synthesis, Molecular-Docking, and Biological Evaluation of Thiazolopyrimidine Carboxylates as Potential Antidiabetic and Antibacterial Agents</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Iram%20Batool">Iram Batool</a>, <a href="https://publications.waset.org/abstracts/search?q=Aamer%20Saeed"> Aamer Saeed</a>, <a href="https://publications.waset.org/abstracts/search?q=Irfan%20Zia%20Qureshi"> Irfan Zia Qureshi</a>, <a href="https://publications.waset.org/abstracts/search?q=Ayesha%20Razzaq"> Ayesha Razzaq</a>, <a href="https://publications.waset.org/abstracts/search?q=Saima%20Kalsoom"> Saima Kalsoom</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Heterocyclic compounds analogues and their derivatives have attracted strong interest in medicinal chemistry due to their biological and pharmacological properties. A series of new thiazolopyrimidine carboxylates were conveniently synthesized by one-pot three-component reaction of ethyl acetoacetate, 2-aminothiazole and benzaldehyde substituted with electron-donating and electron-withdrawing groups in order to find some more potent antidiabetic and antibacterial drugs. The structures of synthesized compounds were characterized by elemental analysis, IR, 1H NMR, 13C NMR spectroscopy. An in vitro antidiabetic effect was evaluated in adult male BALB/c mice and antibacterial activities were tested against Micrococcus luteus, Salmonella typhimurium, Bacillus subtilis, Bordetella bronchiseptica and Escherichia coli. Some of the tested compounds proved to possess good to excellent activities more than the reference drugs. An in silico molecular docking was also performed on synthesized compounds. The current study is expected to provide useful insights into the design of antidiabetic and antibacterial drugs and understanding the mechanism by which such drugs interact with RNA and diabetes target and exert their biochemical action. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=antidiabetic" title="antidiabetic">antidiabetic</a>, <a href="https://publications.waset.org/abstracts/search?q=antibacterial" title=" antibacterial"> antibacterial</a>, <a href="https://publications.waset.org/abstracts/search?q=MOE%20docking" title=" MOE docking"> MOE docking</a>, <a href="https://publications.waset.org/abstracts/search?q=thiazolopyrimidine" title=" thiazolopyrimidine"> thiazolopyrimidine</a> </p> <a href="https://publications.waset.org/abstracts/24188/synthesis-molecular-docking-and-biological-evaluation-of-thiazolopyrimidine-carboxylates-as-potential-antidiabetic-and-antibacterial-agents" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/24188.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">458</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">2145</span> In Silico Exploration of Quinazoline Derivatives as EGFR Inhibitors for Lung Cancer: A Multi-Modal Approach Integrating QSAR-3D, ADMET, Molecular Docking, and Molecular Dynamics Analyses</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Mohamed%20Moussaoui">Mohamed Moussaoui</a> </p> <p class="card-text"><strong>Abstract:</strong></p> A series of thirty-one potential inhibitors targeting the epidermal growth factor receptor kinase (EGFR), derived from quinazoline, underwent 3D-QSAR analysis using CoMFA and CoMSIA methodologies. The training and test sets of quinazoline derivatives were utilized to construct and validate the QSAR models, respectively, with dataset alignment performed using the lowest energy conformer of the most active compound. The best-performing CoMFA and CoMSIA models demonstrated impressive determination coefficients, with R² values of 0.981 and 0.978, respectively, and Leave One Out cross-validation determination coefficients, Q², of 0.645 and 0.729, respectively. Furthermore, external validation using a test set of five compounds yielded predicted determination coefficients, R² test, of 0.929 and 0.909 for CoMFA and CoMSIA, respectively. Building upon these promising results, eighteen new compounds were designed and assessed for drug likeness and ADMET properties through in silico methods. Additionally, molecular docking studies were conducted to elucidate the binding interactions between the selected compounds and the enzyme. Detailed molecular dynamics simulations were performed to analyze the stability, conformational changes, and binding interactions of the quinazoline derivatives with the EGFR kinase. These simulations provided deeper insights into the dynamic behavior of the compounds within the active site. This comprehensive analysis enhances the understanding of quinazoline derivatives as potential anti-cancer agents and provides valuable insights for lead optimization in the early stages of drug discovery, particularly for developing highly potent anticancer therapeutics <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=3D-QSAR" title="3D-QSAR">3D-QSAR</a>, <a href="https://publications.waset.org/abstracts/search?q=CoMFA" title=" CoMFA"> CoMFA</a>, <a href="https://publications.waset.org/abstracts/search?q=CoMSIA" title=" CoMSIA"> CoMSIA</a>, <a href="https://publications.waset.org/abstracts/search?q=ADMET" title=" ADMET"> ADMET</a>, <a href="https://publications.waset.org/abstracts/search?q=molecular%20docking" title=" molecular docking"> molecular docking</a>, <a href="https://publications.waset.org/abstracts/search?q=quinazoline" title=" quinazoline"> quinazoline</a>, <a href="https://publications.waset.org/abstracts/search?q=molecular%20dynamic" title=" molecular dynamic"> molecular dynamic</a>, <a href="https://publications.waset.org/abstracts/search?q=egfr%20inhibitors" title=" egfr inhibitors"> egfr inhibitors</a>, <a href="https://publications.waset.org/abstracts/search?q=lung%20cancer" title=" lung cancer"> lung cancer</a>, <a href="https://publications.waset.org/abstracts/search?q=anticancer" title=" anticancer"> anticancer</a> </p> <a href="https://publications.waset.org/abstracts/186166/in-silico-exploration-of-quinazoline-derivatives-as-egfr-inhibitors-for-lung-cancer-a-multi-modal-approach-integrating-qsar-3d-admet-molecular-docking-and-molecular-dynamics-analyses" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/186166.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">48</span> 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