Binding interactions of vancomycin tracers with a bacterial cell wall peptidoglycan analogue.
Binding interactions between several vancomycin tracers and (N,N'-diacetyl)KDADA in solution were evaluated in a competition format using a surface plasmon resonance instrument. Tracers derivatized from the carboxy terminus or the N-vancosaminyl sugar moiety of vancomycin bind the peptide with an affinity similar to that of underivatized vancomycin. In contrast, N-methylleucyl derivatized vancomycin tracers bind the peptide with a reduced affinity relative to vancomycin.
Department of Chemistry, Abbott Laboratories, Abbott Park, IL 60064-6016, USA. maciej.adamczyk@abbott.com
M
M
Adamczyk
J
J
Grote
J A
JA
Moore
S D
SD
Rege
Z
Z
Yu
D000900:Anti-Bacterial Agents / Q000138:chemical synthesis / Q000737:chemistry / Q000493:pharmacokinetics*; D001419:Bacteria; D001665:Binding Sites; D002473:Cell Wall; D015195:Drug Design; D007700:Kinetics; D015394:Molecular Structure; D010457:Peptidoglycan / Q000737:chemistry*; D011487:Protein Conformation; D013329:Structure-Activity Relationship; D014640:Vancomycin / Q000031:analogs & derivatives* / Q000138:chemical synthesis / Q000737:chemistry / Q000493:pharmacokinetics*
D000900:Anti-Bacterial Agents; D010457:Peptidoglycan; D014640:Vancomycin