Reduction of Helical Content by Insertion of a Disulfide Bond Leads to an Antimicrobial Peptide with Decreased Hemolytic Activity



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CAPs off to the S–S bond: Application of a strategy involving the introduction of intramolecular disulfide bonds to amphipathic cationic antimicrobial peptides (CAPs) led to decreased α-helicity and hydrophobicity. The mutant peptides were observed to have significantly increased (250-fold) minimum hemolytic concentrations while maintaining MIC values against E. coli, affording more therapeutically selective CAPs.