Modulation of supramolecular self-assembly of an antimicrobial designer peptide by single amino acid substitution: implications on peptide activity

Abstract

Hydrophobicity and charge are key properties of antimicrobial peptides (AMPs). We compared the self-assembly performance and its correlation with antimicrobial activity of a designer AMP and analogues with substitution of hydrophobic or cationic residues by alanine. Peptides that formed supramolecular self-assemblies under the studied conditions were those that have higher antimicrobial potency.