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

Organic & Biomolecular Chemistry Pub Date: 2018-06-27 DOI: 10.1039/C8OB00483H

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.

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