Ontology highlight
ABSTRACT:
SUBMITTER: Cochrane SA
PROVIDER: S-EPMC5068289 | biostudies-literature | 2016 Oct
REPOSITORIES: biostudies-literature
Cochrane Stephen A SA Findlay Brandon B Bakhtiary Alireza A Acedo Jeella Z JZ Rodriguez-Lopez Eva M EM Mercier Pascal P Vederas John C JC
Proceedings of the National Academy of Sciences of the United States of America 20160929 41
Tridecaptin A<sub>1</sub> (TriA<sub>1</sub>) is a nonribosomal lipopeptide with selective antimicrobial activity against Gram-negative bacteria. Here we show that TriA<sub>1</sub> exerts its bactericidal effect by binding to the bacterial cell-wall precursor lipid II on the inner membrane, disrupting the proton motive force. Biochemical and biophysical assays show that binding to the Gram-negative variant of lipid II is required for membrane disruption and that only the proton gradient is disper ...[more]