期刊
NANOSCALE
卷 11, 期 1, 页码 266-275出版社
ROYAL SOC CHEMISTRY
DOI: 10.1039/c8nr07334a
关键词
-
类别
资金
- National Institute for Dental and Craniofacial Research of the National Institutes of Health [RO1DE026117]
- Ministry of Economy, Industry and Competitiveness of the Spanish Government [EEBB-I-18-13053]
- NSF through the MRSEC program
- National Science Foundation through the National Nano Coordinated Infrastructure Network (NNCI) [ECCS-1542202]
Recent studies have shown that antimicrobial peptides (AMPs) can self-assemble into supramolecular structures, but this has been overlooked as causative of their antimicrobial activity. Also, the higher antimicrobial potency of d-enantiomers compared to l-enantiomers of AMPs cannot always be attributed to their different resistance to protease degradation. Here, we tested all l- and d-amino acid versions of GL13K, an AMP derived from a human protein, to study structural links between the AMP secondary structure, supramolecular self-assembly dynamics, and antimicrobial activity. pH dependence and the evolution of secondary structures were related to a self-assembly process with differences among these AMPs. The two GL13K enantiomers formed analogous self-assembled twisted nanoribbon structures, but d-GL13K initiated self-assembly faster and had notably higher antimicrobial potency than l-GL13K. A non-antimicrobial scrambled amino acid version of l-GL13K assembled at a much higher pH to form distinctively different self-assembled structures than l-GL13K. Our results support a functional relationship between the AMP self-assembly and their antimicrobial activity.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据