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  • Title: Disruption of interactions between hydrophobic residues on nonpolar faces is a key determinant in decreasing hemolysis and increasing antimicrobial activities of α-helical amphipathic peptides.
    Author: Son M, Lee Y, Hwang H, Hyun S, Yu J.
    Journal: ChemMedChem; 2013 Oct; 8(10):1638-42. PubMed ID: 23894079.
    Abstract:
    To design antimicrobial peptides with decrease pore-forming activity in eukaryotic (host) membranes, an amphipathic α-helical model peptide composed of Leu and Lys was modified to probe the balance in antimicrobial and hemolytic activities. Among analogues with broken hydrophobic interactions, L8N derivative exhibited an 8000-fold decrease in hemolytic activity and an eightfold improvement in antimicrobial activity, affording a 64 000-fold increase in therapeutic index against E. coli.
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