Journal
FEBS LETTERS
Volume 589, Issue 16, Pages 2043-2049Publisher
WILEY
DOI: 10.1016/j.febslet.2015.06.020
Keywords
Aptamer; Thrombin; Prothrombin; Surface plasmon resonance; Equilibrium constant; Kinetic constant
Funding
- Russian Science Foundation [14-14-01131]
- Russian Science Foundation [14-14-01131] Funding Source: Russian Science Foundation
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Structural properties determine binding affinities of DNA aptamers specific to thrombin. Our paper is the first to focus on a family of eight G-quadruplex-based aptamers with varied duplex region length (from two to eight base pairs). We have shown that the duplex, which is not the main binding domain, greatly influences the interaction with thrombin and prothrombhi. Furthermore, the affinity of an aptamer to thrombin and prothrombin increases (respectively from 2.7 x 10(-8) M to 5.6 x 10(-10) M and from 1.8 x 10(-5) M to 7.1 x 10(-9) M) with an increase in the number of nucleotide pairs in the duplex region. (C) 2015 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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