Journal
TALANTA
Volume 99, Issue -, Pages 767-773Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.talanta.2012.07.019
Keywords
Affinity constant; Endonuclease resistance; Kinetics; RNA aptamer; Surface plasmon resonance; Tobramycin
Categories
Funding
- Spanish Government
- European Regional Development Fund
- [CTQ2008-02429]
Ask authors/readers for more resources
Establishing an efficient method for evaluating the affinity changes after post-SELEX modification of aptamers is essential for broadening the application of these oligonucleotides in biosensing. This is especially challenging when the ligand is a small molecule. Changes in affinity upon partial or total replacement of 2'-OH with 2'-OMe groups in the ribose moieties of a tobramycin binding RNA aptamer are described. The kinetic profile and binding properties of the different anti-tobramycin aptamers were measured by surface plasmon resonance (SPR) experiments through a real-time binding assay with the antibiotic covalently coupled to the gold sensor. This configuration maximizes the changes associated to the recognition event, which is otherwise undetectable. The results indicated that the modification slightly affects the binding characteristics of the parent RNA, while conferring biological stability to the aptamers against nucleases. (C) 2012 Elsevier B.V. All rights reserved.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available