Structure-Binding Relationships for the Interaction between a Vancomycin Monoclonal Antibody Fab Fragment and a Library of Vancomycin Analogues and Tracers

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• 作者：Maciej Adamczyk ; Jonathan Grote ; Jeffrey A. Moore ; Sushil D. Rege ; and Zhiguang Yu
• 刊名：Bioconjugate Chemistry
• 出版年：1999
• 出版时间：March 1999
• 年：1999
• 卷：10
• 期：2
• 页码：176 - 185
• 全文大小：294K
• 年卷期：v.10,no.2(March 1999)
• ISSN：1520-4812

文摘

A series of vancomycin analogues and tracers were synthesized, and their binding interactions withan anti-vancomycin Fab fragment were evaluated under mass transport limiting conditions usingsurface plasmon resonance detection. Differences observed in binding interactions were utilized todefine the vancomycin structural elements critical for antibody recognition. Major structural regionsof vancomycin shown to play an important role in anti-vancomycin Fab fragment recognition includetwo sugar moieties and one chlorinated phenyl ring. The N-methylleucyl residue, the carboxy terminalresidue, and residues in the peptide-binding region of vancomycin have minimal impact on the anti-vancomycin Fab fragment/vancomycin binding interaction. The selection of an antibody with suchbinding properties plays a critical role in the development of a vancomycin immunoassay that employsstable calibrators and controls.