Improvement of Aptamer Affinity by Dimerization

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...

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Main Authors: Kazunori Ikebukuro, Koji Sode, Ken-ichi Taira, Hijiri Hasegawa
Format: Article
Language:English
Published: MDPI AG 2008-02-01
Series:Sensors
Subjects:
Online Access:http://www.mdpi.com/1424-8220/8/2/1090/
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author Kazunori Ikebukuro
Koji Sode
Ken-ichi Taira
Hijiri Hasegawa
author_facet Kazunori Ikebukuro
Koji Sode
Ken-ichi Taira
Hijiri Hasegawa
author_sort Kazunori Ikebukuro
collection DOAJ
description 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.
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spelling doaj.art-e442660507ae4e84890c51136db43bf82022-12-22T03:59:34ZengMDPI AGSensors1424-82202008-02-018210901098Improvement of Aptamer Affinity by DimerizationKazunori IkebukuroKoji SodeKen-ichi TairaHijiri HasegawaTo 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.http://www.mdpi.com/1424-8220/8/2/1090/Aptamerdimerizationavidity
spellingShingle Kazunori Ikebukuro
Koji Sode
Ken-ichi Taira
Hijiri Hasegawa
Improvement of Aptamer Affinity by Dimerization
Sensors
Aptamer
dimerization
avidity
title Improvement of Aptamer Affinity by Dimerization
title_full Improvement of Aptamer Affinity by Dimerization
title_fullStr Improvement of Aptamer Affinity by Dimerization
title_full_unstemmed Improvement of Aptamer Affinity by Dimerization
title_short Improvement of Aptamer Affinity by Dimerization
title_sort improvement of aptamer affinity by dimerization
topic Aptamer
dimerization
avidity
url http://www.mdpi.com/1424-8220/8/2/1090/
work_keys_str_mv AT kazunoriikebukuro improvementofaptameraffinitybydimerization
AT kojisode improvementofaptameraffinitybydimerization
AT kenichitaira improvementofaptameraffinitybydimerization
AT hijirihasegawa improvementofaptameraffinitybydimerization