دورية أكاديمية
Molecular dynamic simulation reveals spider antimicrobial peptide Latarcin-1 and human eosinophil cationic protein as peptide inhibitors of SARS-CoV-2 variants.
| العنوان: | Molecular dynamic simulation reveals spider antimicrobial peptide Latarcin-1 and human eosinophil cationic protein as peptide inhibitors of SARS-CoV-2 variants. |
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| المؤلفون: | Cao C; Institute of Biothermal Science and Technology, School of Health Science and Engineering, University of Shanghai for Science and Technology, Shanghai, P.R. China.; AI Research Center, Peng Cheng Laboratory, Shenzhen, Guangdong, P.R. China., Mehmood A; State Key Laboratory of Microbial Metabolism, Joint International Research Laboratory of Metabolic and Developmental Sciences, School of Life Sciences and Biotechnology, Shanghai Jiao Tong University, Shanghai, P.R. China., Li D; Institute of Biothermal Science and Technology, School of Health Science and Engineering, University of Shanghai for Science and Technology, Shanghai, P.R. China.; AI Research Center, Peng Cheng Laboratory, Shenzhen, Guangdong, P.R. China. |
| المصدر: | Journal of biomolecular structure & dynamics [J Biomol Struct Dyn] 2024 Jul; Vol. 42 (11), pp. 5858-5868. Date of Electronic Publication: 2023 Nov 08. |
| نوع المنشور: | Journal Article |
| اللغة: | English |
| بيانات الدورية: | Publisher: Taylor & Francis Country of Publication: England NLM ID: 8404176 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1538-0254 (Electronic) Linking ISSN: 07391102 NLM ISO Abbreviation: J Biomol Struct Dyn Subsets: MEDLINE |
| أسماء مطبوعة: | Publication: June 2012- : Oxon, UK : Taylor & Francis Original Publication: Guilderland, NY : Adenine Press, [c1983- |
| مواضيع طبية MeSH: | Molecular Dynamics Simulation* , SARS-CoV-2*/drug effects , Angiotensin-Converting Enzyme 2*/chemistry , Angiotensin-Converting Enzyme 2*/metabolism , Eosinophil Cationic Protein*/chemistry , Eosinophil Cationic Protein*/metabolism , Spike Glycoprotein, Coronavirus*/chemistry , Spike Glycoprotein, Coronavirus*/metabolism , Protein Binding*, Humans ; Molecular Docking Simulation ; COVID-19/virology ; COVID-19 Drug Treatment ; Animals ; Binding Sites ; Antimicrobial Peptides/chemistry ; Antimicrobial Peptides/pharmacology ; Antiviral Agents/chemistry ; Antiviral Agents/pharmacology ; Arthropod Proteins/chemistry |
| مستخلص: | COVID-19 has rapidly proliferated around 180 countries, and new cases are reported frequently. No peptide medication has been developed that can reliably block SARS-CoV-2 infection. The investigation focuses on the crucial host receptors angiotensin-converting enzyme 2 (ACE2) , which can bind receptor-binding domain (RBD) on the SARS-CoV-2 spike protein (S). To investigate the inhibitory effects of human Eosinophil Cationic Protein (hECP) and Latarcin-1 (L1)on SARS-CoV-2 infection, we have selected them as research subjects. Further, we ran extensive molecular dynamics simulations to bring the docked peptide-ACE2 complex into its equilibrium state. The outcomes were then evaluated with g_MMPBSA and interaction analysis. We have also considered the Delta and Omicron variants to examine these peptides' inhibitory effects. The experimental findings revealed an enhanced capability of L1 and hECP as SARS-CoV-2 inhibitors, occupying hot spots and numerous key residues in ACE2. These include ASP30, ASP38, GLU35 and GLU75, which significantly inhibit the binding of RBD and ACE2 and are effective against two common variants in a similar manner. In addition, this study can serve as a springboard for future research on SARS-CoV-2 inhibitors.Communicated by Ramaswamy H. Sarma. |
| فهرسة مساهمة: | Keywords: ACE2; SARS-CoV-2; molecular dynamics; peptide inhibitors; variants |
| المشرفين على المادة: | EC 3.4.17.23 (Angiotensin-Converting Enzyme 2) EC 3.1.27.- (Eosinophil Cationic Protein) 0 (Spike Glycoprotein, Coronavirus) 0 (spike protein, SARS-CoV-2) EC 3.4.17.23 (ACE2 protein, human) 0 (Antimicrobial Peptides) 0 (Antiviral Agents) 0 (Arthropod Proteins) |
| SCR Organism: | SARS-CoV-2 variants |
| تواريخ الأحداث: | Date Created: 20231108 Date Completed: 20240613 Latest Revision: 20240627 |
| رمز التحديث: | 20240627 |
| DOI: | 10.1080/07391102.2023.2274514 |
| PMID: | 37938133 |
| قاعدة البيانات: | MEDLINE |
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Full Text Finder | تدمد: | 1538-0254 |
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| DOI: | 10.1080/07391102.2023.2274514 |