Membrane-disruptive abilities of beta-hairpin antimicrobial peptides correlate with conformation and activity: a 31P and 1H NMR study.

Abstract excerpt

The membrane interaction and solution conformation of two mutants of the beta-hairpin antimicrobial peptide, protegrin-1 (PG-1), are investigated to understand the structural determinants of antimicrobial potency. One mutant, [A(6,8,13,15)] PG-1, does not have the two disulfide bonds in wild-type PG-1, while the other, [Delta(4,18) G10] PG-1, has only half the number of cationic residues. 31P solid-state NMR...

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