Antimicrobial Peptide Mastoparan-AF Kills Multi-Antibiotic Resistant Escherichia coli O157:H7 via Multiple Membrane Disruption Patterns and Likely by Adopting 3-11 Amphipathic Helices to Favor Membrane Interaction.

ABSTRACT: We investigated the antimicrobial activity and membrane disruption modes of the antimicrobial peptide mastoparan-AF against hemolytic Escherichia coli O157:H7. Based on the physicochemical properties, mastoparan-AF may potentially adopt a 3-11 amphipathic helix-type structure, with five to seven nonpolar or hydrophobic amino acid residues forming the hydrophobic face. E. coli O157:H7 and two diarrheagenic E. coli veterinary clinical isolates, which are highly resistant to multiple antibiotics, are sensitive to mastoparan-AF, with minimum inhibitory and bactericidal concentrations (MIC and MBC) ranging from 16 to 32 μg mL^-1 for E. coli O157:H7 and four to eight μg mL^-1 for the latter two isolates. Mastoparan-AF treatment, which correlates pr

SUBMITTER: Lin CH 

PROVIDER: S-EPMC9961542 | biostudies-literature | 2023 Feb

REPOSITORIES: biostudies-literature