Mechanisms underlying the antimicrobial actions of the antimicrobial peptides Asp-Tyr-Asp-Asp and Asp-Asp-Asp-Tyr

The peptides Asp-Tyr-Asp-Asp (DYDD) and Asp-Asp-Asp-Tyr (DDDY) extracted from Dendrobium aphyllum have antimicrobial effects on Escherichia coli, Pseudomonas aeruginosa, and Monilia albicans, but no effects on Bacillus subtilis and Staphylococcus aureus. The effects of a hydrophobic environment on the secondary structures of these molecules were determined using circular dichroism and atomic force microscopy. Although scanning electron microscopy revealed that DDDY was more destructive to membranes than DYDD, both peptides showed antimicrobial effects against three pathogens. The minimum inhibitory concentration (MIC) of DYDD (18.075 mg/mL) against E. coli was higher than that of DDDY (4.519 mg/mL), and the influence of DYDD on the cell surface potential energy of E. coli was also greater (a decrease of 6.4 ± 0.66 mV) than that of DDDY (a decrease of 4.37 ± 0.77 mV). Moreover, the cell membrane damage and content leakage of DYDD-treated E. coli cells were more severe than those observed in the DDDY-treated cells. However, DDDY showed stronger antibacterial activity against P. aeruginosa and M. albicans than DYDD. A molecular dynamic simulation revealed that the mechanisms underlying the interaction between these two peptides and lipid bilayers were remarkably different. Therefore, two separate models were proposed to describe their antimicrobial activities.