Computer Simulation Characterisation of the Coral Antimicrobial Peptide AmAMP1 PT07

To investigate the biological functions of the antimicrobial peptide AmAMP1 PT07 isolated from coral, bioinformatics tools were employed to predict and analyse its physicochemical properties, structural features, amphiphilicity, modification sites and biosafety. The results indicate that the coral antimicrobial peptide AmAMP1 PT07 is a cationic antimicrobial peptide comprising 43 amino acids. Its secondary structure consists of α-helices (53.49%), unfolded regions (41.86%) and β-sheets (4.65%). It has a theoretical isoelectric point of 11.09, lacks transmembrane domains and a signal peptide, and is classified as an intracellular protein. It contains one phosphorylation site, is susceptible to cleavage by 18 proteases, exhibits no protein toxicity, and demonstrates high stability, hydrophilicity and biosafety. This indicates that AmAMP1 PT07 possesses good stability and biosafety, making it suitable for development as a novel biological preservative with potential application value.