Conformational features of receptor binding domain of SARS-CoV-2 in alcohols: A molecular dynamics study

Abstract

The concentrated monohydric alcohols have been the most commonly used in alcohol-based hand sanitizers to control transmission of COVID-19. [1] The molecular level of understanding on the interaction of protein and highly concentrated alcohols is essential to understand the deactivation mechanism of the virus. Generally, protein’s structural stability and biological function is governed by the their dynamic behaviour in the respective solutions. In this work, we performed extensive molecular dynamics simulations and attempts have been made to explore the conformational features and, solvation properties of the receptor binding domain (RBD) of the spike protein in different alcohol solutions. Attention has been given to explore the interactive mechanisms though which the RBD’s active residues might be blocked. We observed that RBD exhibits different conformational flexibilities in the different alcohols and in their mixtures which might lead partial unfolding to prohibit its activation. The detailed interactions have been explored and presented. [2]