LAUSR

Rabies virus (RABV) is neurotropic and infects all warm-blooded animals. The binding of the virus with host cell receptor components is critical for infection. The present study reports the interaction of nicotinic acetylcholine receptor alpha 1 (nAChRα1) peptides with the rabies virus glycoprotein (RABVG) to design potential anti-rabies agents. The nAChRα1peptide sequences from different species (bovine, human and electric fish/torpedo) were synthesized and their secondary structures were characterized using CD spectroscopy. The molecular docking analysis of nAChRα1 peptides with RABVG indicated the involvement of specific domains and their particular amino acid contributions. Bovine peptide (C-32) (docking score of 14146kJ/mol) and torpedo peptide (T-32) (docking score of 13704kJ/mol) were found to interact strongly with RABVG. T-32 peptides had the highest binding and inhibiting property against RABV compared to other peptide sequences. The results of both computational and experimental methods demonstrated that nAChRα1 peptides and their analogs may serve as potential antiviral agents against RABV infection.