Bioinformatics-Based Prediction of the Structural Characteristics and Antimicrobial Activity of the Peptide Anisaxin-2S

College of Marine and Environmental Sciences, Tianjin University of Science and Technology, Tianjin, 300457, China

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Abstract

Antimicrobial peptides (AMPs) have emerged as promising alternatives to conventional antibiotics for combating antimicrobial resistance. In this study, the marine-derived peptide Anisaxin-2S was systematically analyzed using bioinformatics approaches to investigate its structural characteristics and potential mechanism of action. Physicochemical properties and structural features were predicted using ProtParam, SOPMA, and Swiss-model, while amphipathicity was evaluated with ProtScale and HeliQuest. Molecular docking was further performed to explore its interaction with filamenting temperature-sensitive protein Z (FtsZ), a key regulator of bacterial cell division. The results showed that Anisaxin-2S is a small cationic peptide with good stability and thermal stability. It predominantly adopts an α-helical structure with distinct amphipathic distribution, facilitating its interaction with bacterial membranes and leading to membrane disruption. Moreover, docking analysis indicated that Anisaxin-2S can stably bind to the active region of FtsZ, with hydrogen bonding contributing to the stability of the complex. These findings suggest that Anisaxin-2S exerts antibacterial activity through a dual mechanism involving membrane disruption and intracellular targeting.