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Thermodynamics and Kinetics of Unfolding of Antiparallel G-Quadruplexes in Anti-Thrombin Aptamersстатья
- Авторы: Spiridonova Vera A., Naumova Yulia O., Nikolaeva Polina A., Novikova Tatiana M., Kolomijtseva Galina Ya
- Журнал: Biochemistry (Moscow)
- Том: 87
- Номер: 11
- Год издания: 2022
- Издательство: Pleiades Publishing, Ltd
- Местоположение издательства: Road Town, United Kingdom
- Первая страница: 1292
- Последняя страница: 1300
- Оригинальные версии: Термодинамика и кинетика разворачивания антипараллельных G-квадруплексов в аптамерах к тромбину
- DOI: 10.1134/s0006297922110086
- Аннотация: The process of unfolding of G-quadruplex structure in the RE31 DNA-aptamer and in its complex with thrombin under the action of the fluorescently labeled complementary oligonucleotides of varying length with formation of doublehelix structures has been studied. It has been suggested that G-quadruplex unfolding involves formation of an intermediate complex with an oligonucleotide. Thermodynamic parameters and kinetics of unfolding of the free aptamer and its complex with thrombin differ. Extension of the oligonucleotide sequence complementary to G-quadruplex by two nucleotides to cover the so-called “hinge region” had little impact on the conformational transition of G-quadruplex of the free aptamer. However, a pronounced effect has been observed for the aptamer–protein complex. Most likely these differences could be explained by the thrombin-induced conformational transition of the aptamer involving the hinge region.
- Добавил в систему: Антохина Оксана Геннадьевна