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- W2563345706 abstract "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." @default.
- W2563345706 created "2017-01-06" @default.
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- W2563345706 creator A5070074639 @default.
- W2563345706 creator A5072500902 @default.
- W2563345706 creator A5091055883 @default.
- W2563345706 date "2017-01-20" @default.
- W2563345706 modified "2023-10-01" @default.
- W2563345706 title "Simplified AIP-II Peptidomimetics Are Potent Inhibitors of<i>Staphylococcus aureus</i>AgrC Quorum Sensing Receptors" @default.
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- W2563345706 doi "https://doi.org/10.1002/cbic.201600516" @default.
- W2563345706 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/5505641" @default.
- W2563345706 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/28006082" @default.
- W2563345706 hasPublicationYear "2017" @default.
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