Molecular investigation of antimicrobial peptides againstproteins using a peptide-protein docking approach.

The impact ofresistance on patient's treatment failure is a major concern. Therefore, the development of novel or alternative therapies foris urgently needed. The purpose of this study was to investigate the molecular interactions of various antimicrobial peptides (AMPs) toproteins. We performed the peptide-protein molecular docking using HADDOCK 2.4 webserver. Fourteen AMPs were tested for their binding efficacy against fourproteins. Simulation of the peptide-protein complex was performed using molecular dynamic software package AMBER20. From molecular docking analysis, five peptides (LL-37, Tilapia piscidin 4, napin, snakin-1 and EcAMP1) showed strong binding interactions againstproteins. The strongest binding affinity was observed in the interactions between Snakin-1 and PBP2, TP4 and type I HopQ and EcAMP1 and type I HopQ with -11.1, -13.6 and -13.8 kcal/mol, respectively. The dynamic simulation was performed for two complexes (snakin1-PBP2 and EcAMP1-HopQ). Results of the dynamics simulation showed that EcAMP1 had stable interaction and binding to type I HopQ protein without significant structural changes. In conclusion, both results of docking and simulation showed that EcAMP1 might be useful as a potential therapeutic agent fortreatment. This molecular approach provides deep understanding of the interaction insights between AMPs andproteins. It paves the way for the development of novel anti-using antimicrobial peptides.