期刊
LANGMUIR
卷 28, 期 3, 页码 1846-1851出版社
AMER CHEMICAL SOC
DOI: 10.1021/la2030044
关键词
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资金
- Ministry of Education, Culture, Sports, Science and Technology Japan [20106008]
- Grants-in-Aid for Scientific Research [20106008] Funding Source: KAKEN
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): similar to 2.6 times) and the dissociation constant (K-D) became much smaller (K-D(M): 1.0 x 10(-6):,similar to 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.
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