
In silico screening of known small molecules to bind ACE2 specific RBD on Spike glycoprotein of SARS-CoV-2 for repurposing against COVID-19 [version 1; peer review: 2 approved]
Abstract
Source: F1000Research 2020, 9:663 Last updated: 04 AUG 2020
PHYTOCHEMICAL TO INTERACT WITH NLS BINDING SITE ON IMA3 TO INHIBIT IMPORTIN Α/Β1 MEDIATED NUCLEAR IMPORT OF SARS-COV-2 CARGO
Abstract
Objective:
Ivermectin is an FDA-approved, broad-spectrum anti-parasitic agent. It was originally identified as an inhibitor of interaction between the human 29 immunodeficiency virus-1 (HIV-1) integrase protein (IN) and the Importin (IMP) α/β1 30 heterodimers, which are responsible for IN nuclear import. Recent studies demonstrate that ivermectin is worthy of further consideration as a possible SARS-CoV-2 antiviral.
Methods:
We built the pathogen-host interactome and analyzed, it using PHISTO. We compared Ivermectin and plant molecules for their interaction with Importin α3 (IMA3) using molecular docking studies.
Results:
A phytochemical ATRI001 with the lowest binding energy-7.290 Kcal/mol was found to be superior to Ivermectin with binding energy-4.946 Kcal/mol.
Conclusion:
ATRI001 may be a potential anti-SARS-CoV-2 agent; however, it requires clinical evaluation.
Keywords: Ivermectin, SARS-CoV-2, IMA3, Phytochemical and Molecular docking
Source: International Journal of Pharmacy and Pharmaceutical Sciences
Print ISSN: 2656-0097 | Online ISSN: 0975-1491, Vol 12, Issue 8, 202