title: N-Methyl and peptoid scans of an autoinducing peptide reveal new structural features required for inhibition and activation of AgrC quorum sensing receptors in Staphylococcus aureus.
abstract: We report the first N-methyl and peptoid residue scans of a full-length autoinducing peptide (AIP), AIP-III, used by Staphylococcus aureus for quorum sensing (QS). Biological evaluation of these AIP-III analogues uncovered new features of the AIP-III scaffold that can be tuned to develop chemical probes of QS in all four groups of S. aureus (I-IV).
authors: Department of Chemistry, University of Wisconsin-Madison, 1101 University Avenue, Madison, Wisconsin 53706-1322, USA. blackwell@chem.wisc.edu.
authors: Yftah
authors: Y
authors: Tal-Gan
authors: Danielle M
authors: DM
authors: Stacy
authors: Helen E
authors: HE
authors: Blackwell
mesh_terms: D000900:Anti-Bacterial Agents / Q000737:chemistry* / Q000494:pharmacology; D001426:Bacterial Proteins / Q000819:agonists / Q000037:antagonists & inhibitors / Q000378:metabolism*; D006801:Humans; D008745:Methylation; D034444:Peptoids / Q000737:chemistry* / Q000494:pharmacology; D011494:Protein Kinases / Q000378:metabolism*; D053038:Quorum Sensing / Q000187:drug effects*; D013203:Staphylococcal Infections / Q000382:microbiology; D013211:Staphylococcus aureus / Q000187:drug effects* / Q000502:physiology
chemical_list: D000900:Anti-Bacterial Agents; D001426:Bacterial Proteins; D034444:Peptoids; D011494:Protein Kinases; C531166:AgrC protein, Staphylococcus