Design of Biomolecular Interface for Detecting Carbohydrate and Lectin Weak Interactions

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• 作者：Yukari Sato ; Kyoko Yoshioka ; Teiichi Murakami ; Soichiro Yoshimoto ; Osamu Niwa
• 刊名：Langmuir
• 出版年：2012
• 出版时间：January 24, 2012
• 年：2012
• 卷：28
• 期：3
• 页码：1846-1851
• 全文大小：321K
• 年卷期：v.28,no.3(January 24, 2012)
• ISSN：1520-5827

文摘

A hybrid functional biomolecular interface designed at a molecular size level is very effective at capturing an analyte with high sensitivity even if the interaction is very weak, as when detecting proteins with carbohydrate. We designed and processed a protein (lectin) recognition molecular interface taking the following points into consideration: (1) the height (molecular length) difference between the capturing and spacer molecules; (2) the ratio of capturing molecules in the recognition interface. When the height difference between the maltoside part (Concanavalin A (Con A) recognition group) and the OH group terminated spacer molecules exceeded (>(CH₂)₆), the association rate constant (k_a) became larger (k_a(1/Ms): 2.6 times) and the dissociation constant (K_D) became much smaller (K_D(M): 1.0 脳 10^鈥?: 0.17 times) compared with the similar heights (lengths) of both molecular interfaces. With regard to maltoside density, a 100% maltoside monolayer was unsuitable for detecting Con A. We constructed a nanostructured recognition site with a maltoside part of 10%, which was the most suitable ratio for Con A detection. The binding interaction between Con A and the maltoside group was changed from monovalent binding to bivalent binding when the maltoside part was diluted in the recognition interface. From electrochemical measurements, even though there was a small amount of maltoside component on the suitable recognition monolayer, quality similar to that of 100% maltoside was observed.