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. 2019 Nov 20;14(22):1911-1916.
doi: 10.1002/cmdc.201900460. Epub 2019 Nov 6.

Development of Amphipathic Antimicrobial Peptide Foldamers Based on Magainin 2 Sequence

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Development of Amphipathic Antimicrobial Peptide Foldamers Based on Magainin 2 Sequence

Chihiro Goto et al. ChemMedChem. .

Abstract

Magainin 2 (Mag 2), which is isolated from the skin of frogs, is a representative antimicrobial peptide (AMP), exerts its antimicrobial activity via microbial membrane disruption. It has been reported that both the amphipathicity and helical structure of Mag 2 play an important role in its antimicrobial activity. In this study, we revealed that the sequence of 17 amino acid residues in Mag 2 (peptide 7) is required to exert sufficient activity. We also designed a set of Mag 2 derivatives, based on enhancement of helicity and/or amphipathicity, by incorporation of α,α-disubstituted amino acid residues into the Mag 2 fragment, and evaluated their preferred secondary structures and their antimicrobial activities against both Gram-positive and Gram-negative bacteria. As a result, peptide 11 formed a stable helical structure in solution, and possessed potent antimicrobial activities against both Gram-positive and Gram-negative bacteria without significant cytotoxicity.

Keywords: Amphipathicity; Antimicrobial peptides; Helicity; Hemolysis; α,α-disubstituted amino acids.

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