{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,24]],"date-time":"2026-10-24T20:48:20Z","timestamp":1792874900079,"version":"4.5.0"},"reference-count":58,"publisher":"MDPI AG","issue":"18","license":[{"start":{"date-parts":[[2022,9,13]],"date-time":"2022-09-13T00:00:00Z","timestamp":1663027200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100004686","name":"Deanship of Scientific Research, Vice Presidency for Graduate Studies and Scientific Research, King Faisal University, Saudi Arabia","doi-asserted-by":"publisher","award":["GRANT676"],"award-info":[{"award-number":["GRANT676"]}],"id":[{"id":"10.13039\/501100004686","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Molecules"],"abstract":"<jats:p>New Delhi metallo-\u03b2-lactamase-1 (NDM-1), expressed in different Gram-negative bacteria, is a versatile enzyme capable of hydrolyzing \u03b2-lactam rings containing antibiotics such as penicillins, cephalosporins, and even carbapenems. Multidrug resistance in bacteria mediated by NDM-1 is an emerging threat to the public health, with an enormous economic burden. There is a scarcity in the availability of specific NDM-1 inhibitors, and also a lag in the development of new inhibitors in pharmaceutical industries. In order to identify novel inhibitors of NDM-1, we screened a library of more than 20 million compounds, available at the MCULE purchasable database. Virtual screening led to the identification of six potential inhibitors, namely, MCULE-1996250788-0-2, MCULE-8777613195-0-12, MCULE-2896881895-0-14, MCULE-5843881524-0-3, MCULE-4937132985-0-1, and MCULE-7157846117-0-1. Furthermore, analyses by molecular docking and ADME properties showed that MCULE-8777613195-0-12 was the most suitable inhibitor against NDM-1. An analysis of the binding pose revealed that MCULE-8777613195-0-12 formed four hydrogen bonds with the catalytic residues of NDM-1 (His120, His122, His189, and Cys208) and interacted with other key residues. Molecular dynamics simulation and principal component analysis confirmed the stability of the NDM-1 and MCULE-8777613195-0-12 complex. The in vitro enzyme kinetics showed that the catalytic efficiency (i.e., kcat\/Km) of NDM-1 on various antibiotics decreased significantly in the presence of MCULE-8777613195-0-12, due to poor catalytic proficiency (kcat) and affinity (Km). The IC50 value of MCULE-8777613195-0-12 (54.2 \u00b5M) was comparable to that of a known inhibitor, i.e., D-captopril (10.3 \u00b5M). In sum, MCULE-8777613195-0-12 may serve as a scaffold to further design\/develop more potent inhibitors of NDM-1 and other \u03b2-lactamases.<\/jats:p>","DOI":"10.3390\/molecules27185930","type":"journal-article","created":{"date-parts":[[2022,9,13]],"date-time":"2022-09-13T01:44:03Z","timestamp":1663033443000},"page":"5930","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":19,"title":["Identification of a Potential Inhibitor (MCULE-8777613195-0-12) of New Delhi Metallo-\u03b2-Lactamase-1 (NDM-1) Using In Silico and In Vitro Approaches"],"prefix":"10.3390","volume":"27","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-3328-3559","authenticated-orcid":false,"given":"Ghazala","family":"Muteeb","sequence":"first","affiliation":[{"name":"Department of Nursing, College of Applied Medical Science, King Faisal University, Al-Ahsa 31982, Saudi Arabia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2341-900X","authenticated-orcid":false,"given":"Md Tabish","family":"Rehman","sequence":"additional","affiliation":[{"name":"Department of Pharmacognosy, College of Pharmacy, King Saud University, Riyadh 11451, Saudi Arabia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mohamed F.","family":"AlAjmi","sequence":"additional","affiliation":[{"name":"Department of Pharmacognosy, College of Pharmacy, King Saud University, Riyadh 11451, Saudi Arabia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-1748-2160","authenticated-orcid":false,"given":"Mohammad","family":"Aatif","sequence":"additional","affiliation":[{"name":"Department of Public Health, College of Applied Medical Science, King Faisal University, Al-Ahsa 31982, Saudi Arabia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-1519-9644","authenticated-orcid":false,"given":"Mohd","family":"Farhan","sequence":"additional","affiliation":[{"name":"Department of Basic Sciences, King Faisal University, Al-Ahsa 31982, Saudi Arabia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sheeba","family":"Shafi","sequence":"additional","affiliation":[{"name":"Department of Nursing, College of Applied Medical Science, King Faisal University, Al-Ahsa 31982, Saudi Arabia"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2022,9,13]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","unstructured":"Faheem, M., Rehman, M.T., Danishuddin, M., and Khan, A.U. (2013). Biochemical Characterization of CTX-M-15 from Enterobacter Cloacae and Designing a Novel Non-\u03b2-Lactam-\u03b2-Lactamase Inhibitor. PLoS ONE, 8.","DOI":"10.1371\/annotation\/049bf1aa-d866-471f-95c1-5939d4461f8c"},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"3594","DOI":"10.1080\/07391102.2020.1767209","article-title":"Identifying Novel Inhibitor of Quorum Sensing Transcriptional Regulator (SdiA) of Klebsiella Pneumoniae through Modelling, Docking and Molecular Dynamics Simulation","volume":"39","author":"Ahmed","year":"2021","journal-title":"J. Biomol. Struct. Dyn."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"90","DOI":"10.2174\/1389200217666160727100434","article-title":"Phage Display Technique: A Novel Medicinal Approach to Overcome Antibiotic Resistance by Using Peptide-Based Inhibitors Against \u03b2-Lactamases","volume":"18","author":"Muteeb","year":"2017","journal-title":"Curr. Drug Metab."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"113667","DOI":"10.1016\/j.ejmech.2021.113667","article-title":"Recent Research and Development of NDM-1 Inhibitors","volume":"223","author":"Wang","year":"2021","journal-title":"Eur. J. Med. Chem."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"1050","DOI":"10.1093\/jac\/dki130","article-title":"Revised Ambler Classification of \u03b2-Lactamases","volume":"55","author":"Hall","year":"2005","journal-title":"J. Antimicrob. Chemother."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"969","DOI":"10.1128\/AAC.01009-09","article-title":"Updated Functional Classification of \u03b2-Lactamases","volume":"54","author":"Bush","year":"2010","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"12406","DOI":"10.1038\/ncomms12406","article-title":"Structural Basis of Metallo-\u03b2-Lactamase, Serine-\u03b2-Lactamase and Penicillin-Binding Protein Inhibition by Cyclic Boronates","volume":"7","author":"Brem","year":"2016","journal-title":"Nat. Commun."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"597","DOI":"10.1016\/S1473-3099(10)70143-2","article-title":"Emergence of a New Antibiotic Resistance Mechanism in India, Pakistan, and the UK: A Molecular, Biological, and Epidemiological Study","volume":"10","author":"Kumarasamy","year":"2010","journal-title":"Lancet Infect. Dis."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"9","DOI":"10.1021\/acsinfecdis.8b00247","article-title":"Ten Years with New Delhi Metallo-\u03b2-Lactamase-1 (NDM-1): From Structural Insights to Inhibitor Design","volume":"5","author":"Linciano","year":"2019","journal-title":"ACS Infect. Dis."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"3626","DOI":"10.1021\/jm501844d","article-title":"Approved Drugs Containing Thiols as Inhibitors of Metallo-\u03b2-Lactamases: Strategy To Combat Multidrug-Resistant Bacteria","volume":"58","author":"Klingler","year":"2015","journal-title":"J. Med. Chem."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"386","DOI":"10.1016\/j.bmcl.2013.10.068","article-title":"Simplified Captopril Analogues as NDM-1 Inhibitors","volume":"24","author":"Li","year":"2014","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"ref_12","doi-asserted-by":"crossref","unstructured":"Wang, X., Lu, M., Shi, Y., Ou, Y., and Cheng, X. (2015). Discovery of Novel New Delhi Metallo-\u03b2-Lactamases-1 Inhibitors by Multistep Virtual Screening. PLoS ONE, 10.","DOI":"10.1371\/journal.pone.0118290"},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"80","DOI":"10.1016\/j.jgar.2019.02.003","article-title":"Discovery of NDM-1 Inhibitors from Natural Products","volume":"18","author":"Shi","year":"2019","journal-title":"J. Glob. Antimicrob. Resist."},{"key":"ref_14","doi-asserted-by":"crossref","unstructured":"Iqbal, D., Rehman, M.T., Bin Dukhyil, A., Rizvi, S.M.D., Al Ajmi, M.F., Alshehri, B.M., Banawas, S., Khan, M.S., Alturaiki, W., and Alsaweed, M. (2021). High-Throughput Screening and Molecular Dynamics Simulation of Natural Product-like Compounds against Alzheimer\u2019s Disease through Multitarget Approach. Pharmaceuticals, 14.","DOI":"10.3390\/ph14090937"},{"key":"ref_15","first-page":"1335","article-title":"Celecoxib, Glipizide, Lapatinib, and Sitagliptin as Potential Suspects of Aggravating SARS-CoV-2 (COVID-19) Infection: A Computational Approach","volume":"38","author":"AlAjmi","year":"2021","journal-title":"J. Biomol. Struct. Dyn."},{"key":"ref_16","doi-asserted-by":"crossref","unstructured":"Aatif, M., Muteeb, G., Alsultan, A., Alshoaibi, A., and Khelif, B.Y.B.Y. (2021). Dieckol and Its Derivatives as Potential Inhibitors of SARS-CoV-2 Spike Protein (Uk Strain: VUI 202012\/01): A Computational Study. Mar. Drugs, 19.","DOI":"10.3390\/md19050242"},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"79","DOI":"10.1186\/s13765-020-00564-4","article-title":"Screening Marine Algae Metabolites as High-Affinity Inhibitors of SARS-CoV-2 Main Protease (3CLpro): An in Silico Analysis to Identify Novel Drug Candidates to Combat COVID-19 Pandemic","volume":"63","author":"Muteeb","year":"2020","journal-title":"Appl. Biol. Chem."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"216","DOI":"10.1016\/j.saa.2019.01.090","article-title":"Food Additive Dye (Quinoline Yellow) Promotes Unfolding and Aggregation of Myoglobin: A Spectroscopic and Molecular Docking Analysis","volume":"214","author":"Khan","year":"2019","journal-title":"Spectrochim. Acta Part A Mol. Biomol. Spectrosc."},{"key":"ref_19","doi-asserted-by":"crossref","unstructured":"Shamsi, A., Mohammad, T., Khan, M.S., Shahwan, M., Husain, F.M., Rehman, M.T., Hassan, M.I., Ahmad, F., and Islam, A. (2019). Unraveling Binding Mechanism of Alzheimer\u2019s Drug Rivastigmine Tartrate with Human Transferrin: Molecular Docking and Multi-Spectroscopic Approach towards Neurodegenerative Diseases. Biomolecules, 9.","DOI":"10.3390\/biom9090495"},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"3577","DOI":"10.2174\/1381612826999201116195851","article-title":"Natural Compounds as Inhibitors of SARS-CoV-2 Main Protease (3CLpro): A Molecular Docking and Simulation Approach to Combat COVID-19","volume":"27","author":"Rehman","year":"2020","journal-title":"Curr. Pharm. Des."},{"key":"ref_21","doi-asserted-by":"crossref","unstructured":"Jolliffe, I.T. (1986). Principal Component Analysis for Special Types of Data, Springer.","DOI":"10.1007\/978-1-4757-1904-8"},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"E144","DOI":"10.1111\/j.1469-0691.2012.03796.x","article-title":"NDM-1, OXA-48 and OXA-181 Carbapenemase-Producing Enterobacteriaceae in Sultanate of Oman","volume":"18","author":"Dortet","year":"2012","journal-title":"Clin. Microbiol. Infect."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"356","DOI":"10.1128\/AAC.01194-15","article-title":"Role of Non-Active-Site Residue Trp-93 in the Function and Stability of New Delhi Metallo-\u03b2-Lactamase 1","volume":"60","author":"Khan","year":"2016","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"2093","DOI":"10.1080\/07391102.2019.1627248","article-title":"In Silico Based Unraveling of New Delhi Metallo-\u03b2-Lactamase (NDM-1) Inhibitors from Natural Compounds: A Molecular Docking and Molecular Dynamics Simulation Study","volume":"38","author":"Rahman","year":"2020","journal-title":"J. Biomol. Struct. Dyn."},{"key":"ref_25","doi-asserted-by":"crossref","unstructured":"Rehman, M.T., Alajmi, M.F., Hussain, A., Rather, G.M., and Khan, M.A. (2019). High-Throughput Virtual Screening, Molecular Dynamics Simulation, and Enzyme Kinetics Identified ZINC84525623 as a Potential Inhibitor of NDM-1. Int. J. Mol. Sci., 20.","DOI":"10.3390\/ijms20040819"},{"key":"ref_26","doi-asserted-by":"crossref","unstructured":"Muteeb, G., Alsultan, A., Farhan, M., and Aatif, M. (2022). Risedronate and Methotrexate Are High-Affinity Inhibitors of New Delhi Metallo-\u03b2-Lactamase-1 (NDM-1): A Drug Repurposing Approach. Molecules, 27.","DOI":"10.3390\/molecules27041283"},{"key":"ref_27","doi-asserted-by":"crossref","unstructured":"Wang, Y., Sun, X., Kong, F., Xia, L., Deng, X., Wang, D., and Wang, J. (2020). Specific NDM-1 Inhibitor of Isoliquiritin Enhances the Activity of Meropenem against NDM-1-Positive Enterobacteriaceae in Vitro. Int. J. Environ. Res. Public Health, 17.","DOI":"10.3390\/ijerph17062162"},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"183","DOI":"10.1016\/j.ijantimicag.2011.10.002","article-title":"Emergence of Nosocomial New Delhi Metallo-\u03b2-Lactamase-1 (NDM-1)-Producing Klebsiella Pneumoniae in Patients Admitted to a Tertiary Care Hospital in Kuwait","volume":"39","author":"Jamal","year":"2012","journal-title":"Int. J. Antimicrob. Agents"},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"1484","DOI":"10.1002\/pro.697","article-title":"Crystal Structure of New Delhi Metallo-\u03b2-Lactamase Reveals Molecular Basis for Antibiotic Resistance","volume":"20","author":"King","year":"2011","journal-title":"Protein Sci."},{"key":"ref_30","first-page":"190ra81","article-title":"Silver Enhances Antibiotic Activity Against Gram-Negative Bacteria","volume":"5","author":"Winkler","year":"2013","journal-title":"Sci. Transl. Med."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"5961","DOI":"10.1128\/AAC.01519-12","article-title":"In Vitro and In Vivo Antimicrobial Activities of Gallium Nitrate against Multidrug-Resistant Acinetobacter Baumannii","volume":"56","author":"Antunes","year":"2012","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"860","DOI":"10.1111\/jam.13085","article-title":"In Vitro Evaluation of Metal Chelators as Potential Metallo- \u03b2 -Lactamase Inhibitors","volume":"120","author":"Azumah","year":"2016","journal-title":"J. Appl. Microbiol."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"533","DOI":"10.1021\/acsinfecdis.5b00033","article-title":"Zinc Chelation by a Small-Molecule Adjuvant Potentiates Meropenem Activity in Vivo against NDM-1-Producing Klebsiella Pneumoniae","volume":"1","author":"Falconer","year":"2015","journal-title":"ACS Infect. Dis."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"3054","DOI":"10.1021\/acschembio.8b00743","article-title":"Bioorthogonal Profiling of a Cancer Cell Proteome Identifies a Large Set of 3-Bromopyruvate Targets beyond Glycolysis","volume":"13","author":"Darabedian","year":"2018","journal-title":"ACS Chem. Biol."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"4548","DOI":"10.1111\/bph.14818","article-title":"Pterostilbene Restores Carbapenem Susceptibility in New Delhi Metallo-\u03b2-Lactamase-Producing Isolates by Inhibiting the Activity of New Delhi Metallo-\u03b2-Lactamases","volume":"176","author":"Liu","year":"2019","journal-title":"Br. J. Pharmacol."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"544","DOI":"10.1021\/acsinfecdis.5b00046","article-title":"Bisthiazolidines: A Substrate-Mimicking Scaffold as an Inhibitor of the NDM-1 Carbapenemase","volume":"1","author":"Kosmopoulou","year":"2015","journal-title":"ACS Infect. Dis."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"7267","DOI":"10.1021\/acs.jmedchem.7b00407","article-title":"Dipicolinic Acid Derivatives as Inhibitors of New Delhi Metallo-\u03b2-Lactamase-1","volume":"60","author":"Chen","year":"2017","journal-title":"J. Med. Chem."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"4862","DOI":"10.1021\/jm100213c","article-title":"Mercaptophosphonate Compounds as Broad-Spectrum Inhibitors of the Metallo-\u03b2-Lactamases","volume":"53","author":"Lassaux","year":"2010","journal-title":"J. Med. Chem."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"439","DOI":"10.1038\/s41467-018-02828-6","article-title":"Bismuth Antimicrobial Drugs Serve as Broad-Spectrum Metallo-\u03b2-Lactamase Inhibitors","volume":"9","author":"Wang","year":"2018","journal-title":"Nat. Commun."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"2947","DOI":"10.1016\/j.bmc.2016.04.064","article-title":"Discovery of a Novel Covalent Non-\u03b2-Lactam Inhibitor of the Metallo-\u03b2-Lactamase NDM-1","volume":"24","author":"Christopeit","year":"2016","journal-title":"Bioorg. Med. Chem."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"413","DOI":"10.1021\/acsmedchemlett.5b00495","article-title":"Triazolylthioacetamide: A Valid Scaffold for the Development of New Delhi Metallo-\u03b2-Lactmase-1 (NDM-1) Inhibitors","volume":"7","author":"Zhai","year":"2016","journal-title":"ACS Med. Chem. Lett."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"55","DOI":"10.1021\/cc9800071","article-title":"A Knowledge-Based Approach in Designing Combinatorial or Medicinal Chemistry Libraries for Drug Discovery. 1. A Qualitative and Quantitative Characterization of Known Drug Databases","volume":"1","author":"Ghose","year":"1998","journal-title":"J. Comb. Chem."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"2615","DOI":"10.1021\/jm020017n","article-title":"Molecular Properties That Influence the Oral Bioavailability of Drug Candidates","volume":"45","author":"Veber","year":"2002","journal-title":"J. Med. Chem."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"11362","DOI":"10.1021\/ja303579d","article-title":"New Delhi Metallo-\u03b2-Lactamase: Structural Insights into \u03b2-Lactam Recognition and Inhibition","volume":"134","author":"King","year":"2012","journal-title":"J. Am. Chem. Soc."},{"key":"ref_45","doi-asserted-by":"crossref","unstructured":"Kim, Y., Tesar, C., Mire, J., Jedrzejczak, R., Binkowski, A., Babnigg, G., Sacchettini, J., and Joachimiak, A. (2011). Structure of Apo- and Monometalated Forms of NDM-1-A Highly Potent Carbapenem-Hydrolyzing Metallo-\u03b2-Lactamase. PLoS ONE, 6.","DOI":"10.1371\/journal.pone.0024621"},{"key":"ref_46","doi-asserted-by":"crossref","unstructured":"Shakil, S., Danish Rizvi, S.M., and Greig, N.H. (2021). High Throughput Virtual Screening and Molecular Dynamics Simulation for Identifying a Putative Inhibitor of Bacterial CTX-M-15. Antibiotics, 10.","DOI":"10.3390\/antibiotics10050474"},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"351","DOI":"10.1016\/j.ejmech.2017.05.061","article-title":"Structure-Activity Relationship Study and Optimisation of 2-Aminopyrrole-1-Benzyl-4,5-Diphenyl-1H-Pyrrole-3-Carbonitrile as a Broad Spectrum Metallo-\u03b2-Lactamase Inhibitor","volume":"137","author":"McGeary","year":"2017","journal-title":"Eur. J. Med. Chem."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"4642","DOI":"10.1016\/j.ejmech.2011.08.003","article-title":"Synthesis of Novel 6-Phenyl-2,4-Disubstituted Pyrimidine-5-Carbonitriles as Potential Antimicrobial Agents","volume":"46","author":"Habib","year":"2011","journal-title":"Eur. J. Med. Chem."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"W363","DOI":"10.1093\/nar\/gky473","article-title":"CASTp 3.0: Computed Atlas of Surface Topography of Proteins","volume":"46","author":"Tian","year":"2018","journal-title":"Nucleic Acids Res."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"1750","DOI":"10.1021\/jm030644s","article-title":"Glide: A New Approach for Rapid, Accurate Docking and Scoring. 2. Enrichment Factors in Database Screening","volume":"47","author":"Halgren","year":"2004","journal-title":"J. Med. Chem."},{"key":"ref_51","first-page":"1","article-title":"Identification of Potential Inhibitors of Calcium\/Calmodulin-Dependent Protein Kinase IV from Bioactive Phytoconstituents","volume":"2020","author":"Gupta","year":"2020","journal-title":"Oxid. Med. Cell. Longev."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"6676","DOI":"10.1080\/07391102.2020.1799865","article-title":"Antiviral Potential of Some Novel Structural Analogs of Standard Drugs Repurposed for the Treatment of COVID-19","volume":"39","author":"AlAjmi","year":"2021","journal-title":"J. Biomol. Struct. Dyn."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"111090","DOI":"10.1016\/j.molliq.2019.111090","article-title":"Alpha-Cyclodextrin Turns SDS-Induced Amyloid Fibril into Native-like Structure","volume":"289","author":"Khan","year":"2019","journal-title":"J. Mol. Liq."},{"key":"ref_54","doi-asserted-by":"crossref","unstructured":"AlAjmi, M., Azhar, A., Hasan, S., Alshabr, A., Hussain, A., and Rehman, M.T. (2021). Identification of Natural Compounds (Proanthocyanidin and Rhapontin) as High-Affinity Inhibitor of SARS-CoV-2 Mpro and PLpro Using Computational Strategies. Arch. Med. Sci.","DOI":"10.5114\/aoms\/133706"},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"173","DOI":"10.1016\/j.ijbiomac.2018.05.023","article-title":"Pharmacoinformatics Approach for the Identification of Polo-like Kinase-1 Inhibitors from Natural Sources as Anti-Cancer Agents","volume":"116","author":"AlAjmi","year":"2018","journal-title":"Int. J. Biol. Macromol."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"5083","DOI":"10.1080\/07391102.2020.1784796","article-title":"In Silico Screening of Glycogen Synthase Kinase-3\u03b2 Targeted Ligands against Acetylcholinesterase and Its Probable Relevance to Alzheimer\u2019s Disease","volume":"39","author":"Jabir","year":"2021","journal-title":"J. Biomol. Struct. Dyn."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"205","DOI":"10.1002\/prot.340110305","article-title":"Collective Motions in Proteins: A Covariance Analysis of Atomic Fluctuations in Molecular Dynamics and Normal Mode Simulations","volume":"11","author":"Ichiye","year":"1991","journal-title":"Proteins"},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"20","DOI":"10.1002\/pro.3923","article-title":"The Bio3D Packages for Structural Bioinformatics","volume":"30","author":"Grant","year":"2021","journal-title":"Protein Sci."}],"container-title":["Molecules"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1420-3049\/27\/18\/5930\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T00:30:03Z","timestamp":1760142603000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1420-3049\/27\/18\/5930"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2022,9,13]]},"references-count":58,"journal-issue":{"issue":"18","published-online":{"date-parts":[[2022,9]]}},"alternative-id":["molecules27185930"],"URL":"https:\/\/doi.org\/10.3390\/molecules27185930","relation":{},"ISSN":["1420-3049"],"issn-type":[{"value":"1420-3049","type":"electronic"}],"subject":[],"published":{"date-parts":[[2022,9,13]]}}}