Evaluation of the Therapeutic Potential of Natural Peptides Against Hemagglutinin–Esterase of Bovine Coronavirus Based on Molecular Dynamics Simulation Studies

Abstract

The hemagglutinin–esterase (HE) protein of bovine coronavirus is required for virus attachment and entry into host cells. It is thus an attractive target for the development of peptide‐based antiviral agents. In the present study, molecular docking was performed to identify bioactive peptides with high binding potential toward the HE protein, followed by molecular dynamics (MD) simulations. A total of 16 bioactive peptides were initially evaluated by molecular docking, and 3 peptides with favorable interactions at the HE protein functional site were subsequently subjected to MD simulations. After the simulation run, among the investigated peptides, Peptide 16 exhibited the most favorable interaction with the HE protein. Structural interaction analysis revealed the formation of two salt bridges, two hydrogen bonds, and forty hydrophobic interactions at the binding interface. Furthermore, the averaged MD analyses demonstrated that the HE protein–Peptide 16 (bLFcin f) complex remained structurally stable throughout the simulations. These findings suggest that Peptide 16 is a promising candidate for further experimental evaluation as a peptide inhibitor targeting the HE protein of BCoV.