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Issue 32, 2018
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Evaluation of topologically distinct constrained antimicrobial peptides with broad-spectrum antimicrobial activity

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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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Publication details

The article was received on 26 Feb 2018, accepted on 19 Jun 2018 and first published on 27 Jun 2018


Article type: Paper
DOI: 10.1039/C8OB00483H
Citation: Org. Biomol. Chem., 2018,16, 5764-5770
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    Evaluation of topologically distinct constrained antimicrobial peptides with broad-spectrum antimicrobial activity

    F. Yuan, Y. Tian, W. Qin, J. Li, D. Yang, B. Zhao, F. Yin and Z. Li, Org. Biomol. Chem., 2018, 16, 5764
    DOI: 10.1039/C8OB00483H

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