Inhibitory efficiency of potential drugs against SARS-CoV-2 by blocking human angiotensin converting enzyme-2: Virtual screening and molecular dynamics study. (March 2021)

• Record Type: Journal Article
• Authors: Khan, Abdul Ashik; Baildya, Nabajyoti; Dutta, Tanmoy; Ghosh, Narendra Nath
• Is Part Of: Microbial pathogenesis. Volume 152(2021)
• Publication Date: 2021-03
• Subjects: SARS-CoV-2 -- Molecular dynamics simulation -- ACE-2 -- COVID-19 -- CPM; Pathogenic microorganisms -- Periodicals; Pathology, Molecular -- Periodicals; Communicable Diseases -- microbiology -- Periodicals; Communicable Diseases -- parasitology -- Periodicals; Micro-organismes pathogènes -- Périodiques; Pathologie moléculaire -- Périodiques; Electronic journals; 616.9041
• DOI: 10.1016/j.micpath.2021.104762
• Languages: English
• ISSNs: 0882-4010

Abstract

Abstract: Till date millions of people are infected by SARS-CoV-2 throughout the world, while no potential therapeutics or vaccines are available to combat this deadly virus. Blocking of human angiotensin-converting enzyme 2 (ACE-2) receptor, the binding site of SARS-CoV-2 spike protein, an effective strategy to discover a drug for COVID-19. Herein we have selected 24 anti-bacterial and anti-viral drugs and made a comprehensive analysis by screened them virtually against ACE-2 receptor to find the best blocker by molecular docking and molecular dynamics studies. Analysis of results revealed that, Cefpiramide (CPM) showed the highest binding affinity of −9.1 kcal/mol. Furthermore, MD study for 10 ns and evaluation of parameters like RMSD, RMSF, radius of gyration, solvent accessible surface area analysis confirmed that CPM effectively binds and blocks ACE-2 receptor efficiently. Graphical abstract: Image 1 Highlights: 24 potential anti-viral compounds have been chosen to block the spike ACE2 receptor of SARS-CoV-2. Virtual screening of these drugs showed Cefpiramide (CPM) has highest binding affinity against ACE2. MD-simulation results CPM docked ACE2 showed huge conformational changes within ACE2 cavity. Binding energy analysis between the drug and ACE2 showed there is a huge interaction among themselves.