Characterization of antimicrobial activity and mechanisms of low amphipathic peptides with different α-helical propensity

Acta Biomaterialia
X ZhuAn-Shan Shan

Abstract

Antimicrobial peptides (AMPs) serve as a defense mechanism within multicellular organisms and are attracting increasing attention because of their potential application in the treatment of multidrug-resistant infections. Amphipathicity has long been believed to be the most important consideration for the structural modification and design of both naturally occurring and synthetic AMPs. Previous studies indicated that disruptive amphipathicity formed by replacing the paired charged amino acid residues on the polar face of an amphipathic helix with tryptophan residues linked with hydrogen bonds on the basis of α-helical protein folding principles endowed the AMPs with increased cell selectivity. In an attempt to augment and hone this strategy further, we designed a series of imperfect amphipathic peptides by placing different types of amino acid residues at the hydrogen bond linked positions of α-helix structures to characterize their antimicrobial properties and mechanism of action. The d-Trp-substituted sequence (PRW4-d) showed greater antimicrobial potency than Cys-(C4), Asp-(D4), Ile-(I4), and Pro-(P4) substituted sequences, comparable to the l-Trp-substituted parent sequence (PRW4). Furthermore, the total replacement of Lys ...Continue Reading

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Jul 30, 2015·Acta Biomaterialia·Yujian HuangMingjun Zhang
Jul 24, 2015·Biomolecular Concepts·Małgorzata Cytryńska, Agnieszka Zdybicka-Barabas
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Dec 30, 2021·ACS Applied Materials & Interfaces·Lu ShangFeng Gu

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