Evaluation of topologically distinct constrained antimicrobial peptides with broad-spectrum antimicrobial activity

Organic & Biomolecular Chemistry
Fang YuanZigang Li

Abstract

Antimicrobial peptides (AMPs) are short cationic peptides with a high affinity for membranes and emerged as a promising therapeutic approach with potential for treating infectious diseases. Chemical stabilization of short peptides proved to be a successful approach for enhancing their bio-physical properties. Herein, we designed and synthesized a panel of conformationally constrained antimicrobial peptides with either α-helical or β-hairpin conformation using templating strategies. These synthetic short constrained peptides possess different topological distributions of hydrophobic and hydrophilic residues and displayed distinct antimicrobial activity. Notably, the conformationally constrained α-helical peptides displayed a faster internalization into the bacteria cells compared to their β-hairpin analogues. These synthetic short constrained peptides showed killing effects on a broad spectrum of microorganisms mainly through pore formation and membrane damage which provided a potentially promising skeleton for the next generation of stabilized antimicrobial peptides.

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Citations

Sep 22, 2020·Journal of Materials Chemistry. B, Materials for Biology and Medicine·Yueming WuRunhui Liu

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Methods Mentioned

BETA
circular dichroism
confocal microscopy
scanning electron microscopy

Software Mentioned

K2D3

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