Specific loop modifications of the thrombin-binding aptamer trigger the formation of parallel structures

Anna Aviñó, Guillem Portella, Ruben Ferreira, Raimundo Gargallo, Stefania Mazzini, Valérie Gabelica, Modesto Orozco, Ramon Eritja
  • FEBS Journal, January 2014, Wiley
  • DOI: 10.1111/febs.12670

to fold or to dimerize a dilema for modified TBA

What is it about?

Several years ago it was found a specific DNA sequence known as TBA that is made of 15 nucleotides was able to bind thrombin and become anticoagulant. The structure of this compounds has been described as a folded G-quaduplex in antiparallel orientation. In this paper we show small changes in the sequence that induces a large change in the structure and the modified TBA becomes a dimer G-quadruplex in parallel orientation. Characterization of the new structure was done by CD, UV and MS.

Why is it important?

Quadruplex forming sequences are abundant in the genome. Specially relevant sequecnes capable of forming G-quaplex are found especially in promoter regions of oncogenes and at the end of chormosomes. The conformational diversity of the G-quadruplex structures are an important matter of study as G-quadruplex structures may vary depending of several factors such as ions, crowding agents or dehydrating conditions, pH etc... This work also indicates that mutations in this areas may induce changes.

Read Publication

http://dx.doi.org/10.1111/febs.12670

The following have contributed to this page: Ramon Eritja

In partnership with:

Contributors