Integrating a cationic backbone with a hydrophobic core: A structure-function strategy for designing self-assembling antimicrobial peptides with enhanced activity.

ABSTRACT: Effective countermeasures against multidrug-resistant nosocomial pathogens, such as carbapenem-resistant Klebsiella pneumoniae and methicillin-resistant Staphylococcus aureus (MRSA), require the development of innovative antimicrobial strategies. This study presents a structure-function approach to antimicrobial peptide (AMP) design through the strategic integration of a cationic backbone with a hydrophobic core. This dual-domain architecture enables robust hydrophobic and electrostatic interactions, promoting spontaneous self-assembly and efficient membrane engagement. The lead peptide, Tryptolycin (TRPY), formed stable, monodisperse nanoparticles and demonstrated broad-spectrum bactericidal activity, with minimum inhibitory concentrations ≤1 µmol/L against multiple strains

SUBMITTER: Mwangi J 

PROVIDER: S-EPMC12780499 | biostudies-literature | 2025 Sep

REPOSITORIES: biostudies-literature