Análisis computacional de la interacción in silico de la Agatisflavona con la región de trimerización de la proteína espícula (S) del SARS-CoV-2

Abstract

The spicule (S) glycoprotein is one of the most important proteins for SARS-CoV-2 virus because it plays a critical role in early stages of viral infection and is considered an important molecular target for the development of new drugs or vaccines. In this study we report in silico interaction of the biflavonoid Agathisflavone with the S protein of SARS-CoV-2. For this purpose, molecular docking tests were carried out between Agathisflavone and the spike protein in different conformations (open and closed) in order to determine and characterize the interaction sites and residues involved. Results obtained suggest that Agathisflavone exhibits higher binding affinities for the trimerization site of the viral homotrimer, with favorable binding energy (ΔGb) values of -10.21±0.52 kcal.mol-1 and -11.19±0.16 kcal.mol-1. These findings suggest that the presence of the biflavonoid in interaction with the trimerization region could also act as a blocker of the assembly of the spike into its quaternary structure and could interfere with the viral replicative cycle, therefore, Agathisflavone can be considered for experimental studies.