Mechanistic principles of antimicrobial peptides uncovered by charge density-based machine learning
Abstract
structural compactness, whereas the intermediate-charge/length peptides exhibit balanced hydrophobicity and electrostatics. The high-charge peptides couple strong cationic attraction with lipophilicity and tryptophan anchoring to mainly disrupt membranes. Interestingly, hydrophobic moment, which is a measure of the amphipathicity, is found to be important in all three classes of AMPs. This study identifies distinguishing features of AMP sub-groups and suggests design guidelines for developing selective and potent next-generation AMPs.
Fields of Study & Subjects
Antimicrobial Peptides and Activities
Protein Structure and Dynamics
Biochemical and Structural Characterization
Publication details
- Journal / source
- Chemical Communications
- Publisher
- Royal Society of Chemistry (RSC)
- Volume
- 62
- Issue
- 13
- Pages
- 4067–4070
- Publication date
- 1 January 2026
- Language
- EN