Structure-Activity Study of the Antimicrobial Lipopeptide Humimycin A and Screening Against Multidrug-Resistant <i>Staphylococcus aureus</i>.

ABSTRACT:

Background

The emergence of multidrug-resistant (MDR) Staphylococcus aureus presents a critical global health challenge due to treatment failures and high mortality rates. Faced with this growing threat, new antimicrobials with original modes of action are urgently needed, and antimicrobial peptides proved to be promising alternatives.

Objectives

The aim of this study is to explore the structure-function relationship of the lipopeptide humimycin A, compare the spectrum of activity of the synthetic analogs against a panel of S. aureus isolates, and investigate their binding to the humimycin target, the lipid II flippase MurJ.

Methods

Humimycin A and 15 analogs were produced by solid-phase peptide synthesis, and their antimicrobial activity was evaluated b

SUBMITTER: Rahman MRT 

PROVIDER: S-EPMC12024397 | biostudies-literature | 2025 Apr

REPOSITORIES: biostudies-literature