Understanding the Role of Self-Assembly and Interaction with Biological Membranes of Short Cationic Lipopeptides in the Effective Design of New Antibiotics.

ABSTRACT: This study investigates short cationic antimicrobial lipopeptides composed of 2-4 amino acid residues and C₁₂-C₁₈ fatty acids attached to the N-terminal part of the peptides. The findings were discussed in the context of the relationship among biological activity, self-assembly, stability, and membrane interactions. All the lipopeptides showed the ability to self-assemble in PBS solution. In most cases, the critical aggregation concentration (CAC) much surpassed the minimal inhibitory concentration (MIC) values, suggesting that monomers are the main active form of lipopeptides. The introduction of β-alanine into the peptide sequence resulted in a compound with a high propensity to fibrillate, which increased the peptide stability and activity against S. epidermidis

SUBMITTER: Stachurski O 

PROVIDER: S-EPMC9686977 | biostudies-literature | 2022 Oct

REPOSITORIES: biostudies-literature