Dimerization and membrane anchors in extracellular targeting of vancomycin group antibiotics.
Antibiotics of the vancomycin group are shown to enhance their affinities for the bacterial cell wall by the devices of either dimerization (vancomycin and other glycopeptides which dimerize even more strongly) or use of a membrane anchor (teicoplanin); a chelate mechanism is suggested in both cases, as supported by antagonism experiments with the cell wall analog di-N-acetyl-L-Lys-D-Ala-D-Ala. These results may have implications for other binding processes which occur near membrane surfaces.
Beauregard
D A
DA
Cambridge Centre for Molecular Recognition, University Chemical Laboratory, England.
Williams
D H
DH
Gwynn
M N
MN
Knowles
D J
DJ
D000595:Amino Acid Sequence; D001412:Bacillus subtilis / Q000187:drug effects / Q000648:ultrastructure; D002462:Cell Membrane / Q000378:metabolism; D002473:Cell Wall / Q000187:drug effects; D006860:Hydrogen Bonding; D008969:Molecular Sequence Data; D014640:Vancomycin / Q000737:chemistry* / Q000494:pharmacology*
D014640:Vancomycin