Informace o publikaci

Elongated Thrombin Binding Aptamer: A G-Quadruplex Cation-Sensitive Conformational Switch

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RACHE Aurore De KEJNOVSKÁ Iva VORLÍČKOVÁ Michaela BUESS-HERMAN Claudine

Rok publikování 2012
Druh Článek v odborném periodiku
Časopis / Zdroj Chemistry - A European Journal
Fakulta / Pracoviště MU

Středoevropský technologický institut

Citace
www http://www.sciencedirect.com/science/article/pii/S0925857415000658
Doi http://dx.doi.org/10.1002/chem.201103381
Obor Biofyzika
Klíčová slova circular dichroism; DNA structures; G-quadruplexes; hexa-ammine ruthenium; thermal difference spectra
Popis Aptamer-based biosensors offer promising perspectives for high performance, specific detection of proteins. The thrombin binding aptamer (TBA) is a G-quadruplex-forming DNA sequence, which is frequently elongated at one end to increase its analytical performances in a biosensor configuration. Herein, we investigate how the elongation of TBA at its 5' end affects its structure and stability. Circular dichroism spectroscopy shows that TBA folds in an antiparallel G-quadruplex conformation with all studied cations (Ba2+, Ca2+, K+, Mg2+, Na+, NH4+, Sr2+ and the [Ru(NH3)6]2+/3+ redox marker) whereas other structures are adopted by the elongated aptamers in the presence of some of these cations. The stability of each structure is evaluated on the basis of UV spectroscopy melting curves. Thermal difference spectra confirm the quadruplex character of all conformations. The elongated sequences can adopt a parallel or an antiparallel structure, depending on the nature of the cation; this can potentially confer an ion-sensitive switch behavior. This switch property is demonstrated with the frequently employed redox complex [Ru(NH3)6]3+, which induces the parallel conformation at very low concentrations (10 equiv per strand). The addition of large amounts of K+ reverts the conformation to the antiparallel form, and opens interesting perspectives for electrochemical biosensing or redox-active responsive devices.

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