Abstract— Influenza A viruses pose significant threats to human and animal health due to their capacity for rapid evolution, host adaptation, and pandemic emergence. Among these, the H5N1 subtype is highly pathogenic in birds and remains a critical zoonotic concern. Viral attachment and host specificity are mediated by the hemagglutinin (HA) glycoprotein, whose receptor-binding properties can shift through mutation. In this study, the antiviral potential of two peptides, PLNC8α and PLNC8β, was evaluated in silico against the H5N1 HA protein. Docking analyses revealed that PLNC8β exhibited the strongest binding affinity with a binding energy of –252.86 kcal/mol, compared to –240.47 kcal/mol for PLNC8α. Overall, PLNC8β showed superior binding characteristics, highlighting its promise as a potential antiviral agent against H5N1. Further experimental validation is needed to confirm these computational findings.

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