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Asian Journal of Biochemistry
Year: 2009  |  Volume: 4  |  Issue: 4  |  Page No.: 106 - 116

Entropy Driven Binding of O-Glycan and Glycoproteins to Artocarpus hirsuta Lectin: An SPR Study

F. Khan, S.M. Gaikwad and M.I. Khan    

Abstract: In this study, thermodynamics of binding of O-glycan (Galβ1→3GalNAcα1→OSer) and the glycoproteins possessing it, viz., fetuin and mucin to A. hirsuta lectin was studied using Surface Plasmon Resonance (SPR). The binding affinities were in the order of asialomucin >mucin>asialofetuin>fetuin>O-glycan and found to increase with increase in valency of the ligand. Unusual for a lectin-ligand interaction, the binding was endothermic and entropically driven and the higher affinity was associated with a large favorable entropy term. The native fetuin and mucin showed lower affinity than their desialylated counterpart. Kinetic analysis of the binding revealed that the difference in the affinity of different ligands was due to different rates of their association, whereas the dissociation rates were similar and showed decrease with temperature. The activation energy of the association process was lower with desialylated glycoproteins than that of sialylated one resulting in their faster association and higher affinity.

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