Novel multidomain peptide self-assembly biomaterials based on bola structure and terminal anchoring: Nanotechnology meets antimicrobial therapy.

ABSTRACT: To ameliorate the diminished antimicrobial efficiency and physiological stability associated with monomeric antimicrobial peptides (AMPs) molecules, future research will focus on the artificial design of self-assembling peptides to replace monomeric entities, aiming to combat the antibiotic resistance crisis caused by microbial infections. In this study, the "bola" structure was used as the foundational architecture driving molecular self-assembly, with hydrophobic amino acids at the termini to anchor and finely adjust the sequence, thereby organizing a range of novel multidomain peptides (MDPs) templates into an ABA block motif. The results indicate that FW2 (GM_SI = 53.94) exhibits the highest selectivity index among all MDPs and can form spherical micelles in an aqueous medium

SUBMITTER: Yu W 

PROVIDER: S-EPMC11363844 | biostudies-literature | 2024 Oct

REPOSITORIES: biostudies-literature