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Sensors 2008, 8(2), 1090-1098;

Improvement of Aptamer Affinity by Dimerization

Department of Biotechnology and Life Science, Tokyo University of Agriculture and Technology 2-24-16 Naka-cho, Koganei, Tokyo 184-8588, Japan
Author to whom correspondence should be addressed.
Received: 29 January 2008 / Accepted: 15 February 2008 / Published: 19 February 2008
(This article belongs to the Special Issue Bioanalysis in Vivo/in Vitro)
Full-Text   |   PDF [870 KB, uploaded 21 June 2014]


To increase the affinities of aptamers for their targets, we designed an aptamerdimer for thrombin and VEGF. This design is based on the avidity of the antibody, whichenables the aptamer to connect easily since it is a single-strand nucleic acid. In this study,we connected a 15-mer thrombin-binding aptamer with a 29-mer thrombin-binding aptamer.Each aptamer recognizes a different part of the thrombin molecule, and the aptamer dimerhas a Kd value which is 1/10 of that of the monomers from which it is composed. Also, thedesigned aptamer dimer has higher inhibitory activity than the reported (15-mer) thrombin-inhibiting aptamer. Additionally, we connected together two identical aptamers againstvascular endothelial growth factor (VEGF165), which is a homodimeric protein. As in thecase of the anti-thrombin aptamer, the dimeric anti-VEGF aptamer had a much lower Kd value than that of the monomer. This study demonstrated that the dimerization of aptamerseffectively improves the affinities of those aptamers for their targets. View Full-Text
Keywords: Aptamer; dimerization; avidity Aptamer; dimerization; avidity
This is an open access article distributed under the Creative Commons Attribution License (CC BY 3.0).

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MDPI and ACS Style

Hasegawa, H.; Taira, K.-I.; Sode, K.; Ikebukuro, K. Improvement of Aptamer Affinity by Dimerization. Sensors 2008, 8, 1090-1098.

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