期刊
CHEMBIOCHEM
卷 18, 期 4, 页码 413-423出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/cbic.201600516
关键词
accessory gene regulator; autoinducing peptides; peptidomimetics; quorum sensing; Staphylococcus aureus
资金
- Office of Naval Research [N00014-16-1-2185]
- Kimberly-Clark Corporation
- Burroughs Welcome Fund
- UW-Madison NIH Chemistry-Biology Interface Training Program [T32 GM008505]
- Wisconsin Alumni Research Foundation
- National Science Foundation (NSF) Graduate Research Fellowship [DGE-1256259]
- National Institutes of Health (NIH) [P41 GM103399, P41 GM66326, RR02781, RR08438]
- NSF [DMB-8415048, OIA-9977486, BIR-9214394, CHE-9974839]
- NIH [1S10 OD020022-1, S10 OD012245]
The bacterial pathogen Staphylococcus aureus controls many aspects of virulence by using the accessory gene regulator (agr) quorum sensing (QS) system. The agr system is activated by a macrocyclic peptide signal known as an autoinducing peptide (AIP). We sought to develop structurally simplified mimetics of AIPs for use as chemical tools to study QS in S. aureus. Herein, we report new peptidomimetic AgrC receptor inhibitors based on a tail-truncated AIP-II peptide that have almost analogous inhibitory activities to the parent peptide. Structural comparison of one of these peptidomimetics to the parent peptide and a highly potent, all-peptide-derived, S. aureus agr inhibitor (AIP-III D4A) revealed a conserved hydrophobic motif and overall amphipathic nature. Our results suggest that the AIP scaffold is amenable to structural mimicry and minimization for the development of synthetic agr inhibitors.
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