Structure-binding relationships for the interaction between a vancomycin monoclonal antibody fab fragment and a library of vancomycin analogues and tracers

A series of vancomycin analogues and tracers were synthesized, and their bi nding interactions with an anti-vancomycin Fab fragment were evaluated unde r mass transport Limiting conditions using surface plasmon resonance detect ion. Differences observed in binding interactions were utilized to define t he vancomycin structural elements critical for antibody recognition. Major structural regions of vancomycin shown to play an important role in anti-va ncomycin Fab fragment recognition include two sugar moieties and one chlori nated phenyl ring. The N-methylleucyl residue, the carboxy terminal residue , and residues in the peptide-binding region of vancomycin have minimal imp act on the anti-vancomycin Fab fragment/vancomycin binding interaction. The selection of an antibody with such binding properties plays a critical rol e in the development of a vancomycin immunoassay that employs stable calibr ators and controls.