Angew. Chem. Int. Edit.: Bacteria-Assisted Activation of Antimicrobial Polypeptides by a Random-Coil to Helix Transition

time:2018-03-15Hits:94设置

Title:

Bacteria-Assisted Activation of Antimicrobial Polypeptides by a Random-Coil to Helix Transition

Authors:

Menghua Xiong1, Zhiyuan Han1, Ziyuan Song1, Jin Yu1, Hanze Ying1, Lichen Yin2, and Jianjun Cheng1,2

Institutions:

1Department of Materials Science and Engineering, University of Illinois at Urbana–Champaign, 1304 W. Green Street, Urbana, IL 61801 (USA);

2Jiangsu Key Laboratory for Carbon-Based Functional Materials & Devices, Institute of Functional Nano & Soft Materials, Collaborative Innovation Center of Suzhou Nano Science & Technology, Soochow University, Jiangsu, China 215123;

Abstract:

The application of antimicrobial peptides (AMPs) is largely hindered by their non-specific toxicity against mammalian cells, which is usually associated with helical structure, hydrophobicity, and charge density. A random coil-to-helix transition mechanism has now been introduced into the design of AMPs, minimizing the toxicity against mammalian cells while maintaining high antimicrobial activity. By incorporating anionic phosphorylated tyrosine into the cationic polypeptide, the helical structure of AMPs was distorted owing to the side-chain charge interaction. Together with the decreased charge density, the AMPs exhibited inhibited toxicity against mammalian cells. At the infectious site, the AMPs can be activated by bacterial phosphatase to restore the helical structure, thus contributing to strong membrane disruptive capability and potent antimicrobial activity. This bacteriaactivated system is an effective strategy to enhance the therapeutic selectivity of AMPs.

IF:

11.994

Link:

http://onlinelibrary.wiley.com/doi/10.1002/anie.201706071/full

Editor: Danting Xiang


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