The antimicrobial peptide Magainin-2 interacts with BamA impairing folding of E. coli membrane proteins.

ABSTRACT: Antimicrobial peptides (AMPs) are a unique and diverse group of molecules endowed with a broad spectrum of antibiotics properties that are being considered as new alternative therapeutic agents. Most of these peptides are membrane-active molecules, killing bacteria by membrane disruption. However, recently an increasing number of AMPs was shown to enter bacterial cells and target intracellular processes fundamental for bacterial life. In this paper we investigated the mechanism of action of Maganin-2 (Mag-2), a well-known antimicrobial peptide isolated from the African clawed frog Xenopus laevis, by functional proteomic approaches. Several proteins belonging to E. coli macromolecular membrane complexes were identified as Mag-2 putative interactors. Among these, we focused our

SUBMITTER: Di Somma A 

PROVIDER: S-EPMC9620421 | biostudies-literature | 2022

REPOSITORIES: biostudies-literature