Molecular Docking Approach On Potential Of 2,6-Diphenylpiperidin-4-Ol Derivatives To Inhibit Covid 19 Mainprotease

Abstract

ABSTRACT:

COVID-19 is a disease caused due to SARS-CoV-2, the deadliest global spread of recent years. The virus spreads among humans through any type of contact between each other, through the air, and also through contaminated surfaces. The Main Protease (M^Pro) of  SARS-CoV-2 is one of the expected targets in the development of new drug molecules for the disease. Some drugs like "chloroquine" and "remdesivir" have been used for therapeutics of COVID-19, even though the effect of these compounds is still mysterious. In the present study, the ligand and structure-based study was applied to compute the interaction with 2,6-diphenylpiperidin-4-ol derivatives on COVID-19 main protease. 2,6-diphenylpiperidin-4-ol derivatives (M1-M7) were found to show a similar structure of some Antiviral drugs via Qikprop. In silico docking study was carried out by 2,6-diphenylpiperidin-4-ol derivatives using Schrodinger Maestro 12.4 on SARS-CoV-2 M^Pro receptors with PDB ID of 5R84. The potential imperative energy were calculated and the interactivity of each ligand were analyzed. To further expound the binding sites of the inhibitors for 5R84 active sites of three docking programs such as, Glide Score, Extra Precision (XP) Energy, Glide Energy were used. The attribute of the actively binding sites were then set out by the conformations of  docking results. In conclusion, the 2,6-diphenylpiperidin-4-ol derivative with the best binding energy was noted to have high potency against COVID-19 Mainprotease.