Minimal domain peptides derived from enterocins exhibit potent antifungal activity.

ABSTRACT: The antimicrobial peptide (AMP) circularized bacteriocin enterocin AS-48 produced by Enterococcus sp. exhibits broad-spectrum antibacterial activity via dimer insertion into the plasma membrane to form membrane pore structures, compromising membrane integrity and leading to bactericidal activity. A specific alpha-helical region of enterocin AS-48 has been shown to be responsible for the membrane-penetrating activity of the peptide. The canon syn-enterocin peptide library, generated using rational design techniques to have ninety-five synthetic peptide variants from the truncated, linearized, membrane-interacting domain of enterocin AS-48, was screened against three clinically relevant fungal strains: Cryptococcus neoformans, Candida albicans, and Candida auris f

SUBMITTER: Cohen DG 

PROVIDER: S-EPMC11693670 | biostudies-literature | 2024

REPOSITORIES: biostudies-literature