Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
8304337 | Biochimie | 2016 | 4 Pages |
Abstract
The aptamer d(GGGT)4 (T30923 or T30695) forms a 5â²-5â² dimer of two stacked parallel G-quadruplexes, each characterized by three G-tetrads and three single-thymidine reversed-chain loops. This aptamer has been reported to exhibit anti-HIV activity by targeting the HIV integrase, a viral enzyme responsible for the integration of viral DNA into the host-cell genome. However, information concerning the aptamer/target interaction is still rather limited. In this communication we report microscale thermophoresis investigations on the interaction between the HIV-1 integrase and d(GGGT)4 aptamer analogues containing abasic sites singly replacing thymidines in the original sequence. This approach has allowed the identification of which part of the aptamer G-quadruplex structure is mainly involved in the interaction with the protein.
Related Topics
Life Sciences
Biochemistry, Genetics and Molecular Biology
Biochemistry
Authors
Veronica Esposito, Luciano Pirone, Luciano Mayol, Emilia Pedone, Antonella Virgilio, Aldo Galeone,