期刊
MICROBIAL BIOTECHNOLOGY
卷 14, 期 2, 页码 656-667出版社
WILEY
DOI: 10.1111/1751-7915.13721
关键词
-
资金
- National Natural Science Foundation of China [81970928, 81570967]
- Guangdong Basic and Applied Basic Research Foundation [2019A1515110847]
This study simulated short amyloid-forming peptides derived from Streptococcus mutans and found that they have efficient broad-spectrum antibiofilm activity against various bacteria and fungi, by aggregating into amyloid fibres. The peptides bind to microbial cell wall carbohydrates and trigger significant fibrillation, highlighting their potential use as novel antibiofilm agents.
Evidence suggests that short amyloid-forming peptides derived from bacterial proteomes have functional roles; however, the reported activities are diverse and the underlying mechanisms remain unclear. In this study, we simulated short amyloid-forming peptides from the amyloid-forming truncated protein C123 of Streptococcus mutans (S. mutans), studied their biological functions in microbial proliferation and biofilm formation, and further investigated the underlying mechanism. Fourteen hexapeptides were simulated, 13 of which were successfully synthesized. We found that the amyloid-forming hexapeptides (AFhPs) displayed efficient broad-spectrum antibiofilm activity against the Gram-positive bacteria S. mutans, Streptococcus sanguis and Staphylococcus aureus, Gram-negative bacteria Escherichia coli and fungus Candida albicans, by aggregating into rigid amyloid fibres agglutinating microbes, whereas the non-amyloid-forming hexapeptides (non-AFhPs) did not. The AFhPs did not kill microbes and showed little or no cytotoxicity. Furthermore, a set of AFhPs displayed broad-spectrum antibiofilm activity, regardless of its source. The microbial cell wall carbohydrates, peptidoglycan (PGN), lipoteichoic acid (LTA), glucan and zymosan A, mediated AFhP binding and triggered significant AFhP fibrillation. Although amyloid fibres agglutinated lipid membrane model - large unilamellar vesicles (LUVs) - and LUVs facilitated AFhP fibrillation, the roles of lipid membranes in AFhP antibiofilm activities remain to be elucidated. We highlight the potential use of AFhPs as novel antibiofilm agents.
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