Keywords : Nuraminidase
Molecular docking of novel, short peptide from Flammulina velutipes with influenza drug targets in comparison with anti-influenza drugs amantadine, oseltamivir and zanamivir
karbala journal of pharmaceutical sciences,
Volume 5, Issue 8, Pages 1-10
Influenza viruses known to cause widespread morbidity and mortality, and distributed throughout several parts of the world, producing a serious public health threat, and may result in a pandemic. The antimicrobial peptides known to have broad spectrum activity and considered a promising agents in microbial inhibition and killing. So that this study was done to find the probable scope of anti-influenza activity of short peptide FV16 (KKVGTSKVVAKTVTKK) a sixteen amino acids short peptide inspired from the bacteria F. velutipes. Hex 8.0.0 software was used to find the probable binding positions and binding strength of FV16 with particular viral targets. This study was resulted in a high degree of binding strength of FV16 with the most studied influenza targets in comparison with the binding strength of other approved anti-influenza drugs (amantadine, oseltamivir and zanamivir), the influenza drug targets were neuraminidase, hemagglutinin, M1 and M2 proteins. Furthermore, FV16 binding positions on each particular viral targets derived from particular strain have its own unique position, this may give it the property of multi-strain binding agent to expand its spectrum against influenza virus strains. In conclusion, FV16 may have the potential to be an anti-influenza agent, and may bind to future generated strains. Future in vitro studies needed to prove this hypothesis.