Reaction pathway and free energy profile determined for specific recognition of oligosaccharide moiety of carboxypeptidase Y

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• 作者：El偶bieta Senkara-Barwijuk^a ; Tomasz Kobiela^a ; ^{kobiela@ch.pw.edu.pl} ; Kateryna Lebed^b ; Ma艂gorzata Lekka^b
• 关键词：Atomic force microscopy ; Quartz crystal microbalance ; Lectin-carbohydrate interaction
• 刊名：Biosensors and Bioelectronics
• 出版年：2012
• 期刊代码：12_09565663
• 类别：ch
• 出版时间：June-July, 2012
• 卷：36
• 期：1
• 页码：103-109
• 文件大小：551 K

摘要

The interaction of mannose specific lectin (from Lens culinaris, LcL) with the carbohydrate moiety of carboxypeptidase Y (CaY) was studied using both atomic force microscope (AFM) and quartz crystal microbalance with dissipation monitoring (QCM-D). The AFM enables to determine the positions of energy barriers present in the energy landscape of the single complex undergoing dissociation. The QCM-D measurements allow the estimation of the quantitative parameters characterizing the kinetics of the studied molecular interaction (namely the association and dissociation rate constants and the association constant). The use of both methods not only delivers the complementary characterization of kinetic and thermodynamic parameters but also permits to investigate the mechanism of the binding and unbinding of the molecules. The results for LcL were compared with those obtained for concanavalin A i.e. lectin, which interacts with the carbohydrate moiety on a similar way.