Insights on Anthocyanidins’ Binding Affinity and Molecular Interactions with Zika Virus Protein Targets

Abstract

Neonatal microencephaly and some neurological disorders have been associated with Zika virus (ZikV) infection. In recent years, the pathophysiology of ZikV was well elucidated; hence, different drug targets have been proposed to inhibit its activities. However, there has been no approved drug against ZikV infection to date. This paper examined the binding affinity and non-covalent binding interactions of the different classes of anthocyanidins against ZikV drug targets. Anthocyanidins are plant pigments, where their bio-functionalities are reasonably well studied. Anthocyanidins and their derivatives have shown antiviral properties; however, their mechanism against ZikV remains elusive. Through in silico molecular docking, this paper illuminates the understanding of these compounds’ binding interactions and binding energies with the different ZikV protein drug targets, namely NS3 helicase, NS2B-NS3 protease, NS5 methyltransferase, NS5 polymerase, and Axl kinase. Results have shown that anthocyanidins generally have a higher binding affinity with NS5 methyltransferase compared to the others. Also, the top-binding anthocyanidin differs in each protein. This paper hypothesized that the inhibitory potential of the different classes of anthocyanidins might differ due to the contrasting binding interactions with the various ZikV protein drug targets.