Antifouling performance of d-enantiomers-based peptide-modified aluminum alloy surfaces with enhanced stability against proteolytic degradation.

Marine biofouling presents a significant challenge to the sustainable development of the maritime industry. Antimicrobial peptide (AMP) offers a promising strategy to combat biofouling. However, the inherent susceptibility of natural AMPs composed of L-amino acids to proteolytic degradation limits their practical application. This study investigated the stability of peptides containing d-amino acids against proteolytic degradation and evaluated their antifouling performance through the modification of aluminum-based surfaces with these peptides. d-peptides exhibited remarkable stability compared to the l-peptides counterpart when exposed to pepsin. Furthermore, the surfaces modified with d-peptides displayed excellent antifouling capacity by significantly inhibiting the adhesion of Bacillus sp. (58.6%) and E. coli (88.7%), the comparable effects observed with l-peptides (61.7%) and (87.5%), respectively. Coarse-grained molecular dynamics simulations and scanning electron microscopy results analyses revealed that immobilized d-peptides effectively disrupted bacterial cell membranes, thereby preventing bacterial adhesion. This research provided a viable approach to enhance the stability of peptides against proteolytic degradation while maintaining outstanding antifouling performance, contributing to the development of effective strategies for antifouling in the maritime industry. [ABSTRACT FROM AUTHOR]