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Investigation of glycopolymer–lectin interactions using QCM-d: comparison of surface binding with inhibitory activity

Year: 2012

Journal: Polym. Chem., 2012,3, 1634-1640, 20120618

Authors: Yanzi Gou , Sarah-Jane Richards , David M. Haddleton and Matthew I. Gibson

Last authors: Matthew I. Gibson

Organizations: Department of Chemistry, University of Warwick, Gibbet Hill Road, Coventry, UK

Country: UK, England, United Kingdom, Great Britain

Glycopolymers offer many opportunities for interfacing synthetic materials with biological systems. However, the nature of the interactions between glycopolymers and their biological targets, lectins, and the structural features necessary to obtain high-affinity materials are not fully understood. Here, the enhancement in binding affinity of multivalent glycopolymers to their corresponding lectins is investigated by quartz-crystal microbalance with dissipation monitoring (QCM-d). This technique allows the conformation of the adsorbed polymers to be probed and the direct observation of spanning of multiple binding sites on lectin-functional surfaces. The measured affinity was compared to the anti-adhesion activity of the polymers in solution, and it is shown that increased association constants did not directly correlate with inhibitory activity.