English   español  
Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/48054
Share/Impact:
Statistics
logo share SHARE logo core CORE   Add this article to your Mendeley library MendeleyBASE

Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL
Exportar a otros formatos:
Title

Evaluation of the structure–activity relationship of thrombin with thrombin binding aptamers by voltammetry and atomic force microscopy

AuthorsDiculescu, Victor Constantin; Chiorcea-Paquim, Ana-Maria; Eritja Casadellà, Ramón; Oliveira-Bret, Ana Maria
KeywordsThrombin
Aptamer
Quadruplex
Guanine
AFM
Electrochemistry
Issue Date15-Jun-2011
PublisherElsevier
CitationJournal of Electroanalytical Chemistry 656(1–2): 159–166 (2011)
AbstractThe structure–activity relationship of the complex between thrombin and thrombin binding aptamers (TBA) was evaluated by differential pulse voltammetry at a glassy carbon electrode and atomic force microscopy at a highly oriented pyrolytic graphite electrode. The effects on the interaction with thrombin of TBA primary and secondary structures as well as of its folding properties in the presence of alkaline metals were investigated. The complex between thrombin and single stranded aptamers involved the coiling of the single stranded molecules around thrombin structure leading to the formation of a robust TBA–thrombin complex that maintains the symmetry and conformation of the thrombin molecule. Monitoring both thrombin and TBA oxidation peaks, showed that the thrombin oxidation peaks occur at more positive potentials after TBA–thrombin complex formation. In the presence of K+ ions, the aptamers fold into quadruplex structures that facilitate the interaction with thrombin molecules. The TBA–thrombin complex adsorbs at the surface with the aptamer quadruplex always in preferential contact with the surface, and the thrombin molecules on top of the aptamer quadruplex structure, thus being less accessible to the electrode surface leading to the occurrence of thrombin oxidation peaks at less positive potentials.
Publisher version (URL)http://dx.doi.org/10.1016/j.jelechem.2010.11.037
URIhttp://hdl.handle.net/10261/48054
DOI10.1016/j.jelechem.2010.11.037
ISSN1572-6657
Appears in Collections:(IQAC) Artículos
Files in This Item:
File Description SizeFormat 
evaluation_structure-activity_Diculescu.pdf1,22 MBAdobe PDFThumbnail
View/Open
Show full item record
Review this work
 

Related articles:


WARNING: Items in Digital.CSIC are protected by copyright, with all rights reserved, unless otherwise indicated.