Exploring the binding of d(GGGT)4 to the HIV-1 integrase: An approach to investigate G-quadruplex aptamer/target protein interactions.
The aptamer d(GGGT)4 (T30923 or T30695) forms a 5'-5' 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.
Dipartimento di Farmacia, Università di Napoli federico II, Via D. Montesano 49, 80131, Napoli, Italy.
Veronica
V
Esposito
Istituto di Biostrutture e Bioimmagini, CNR, Via Mezzocannone 16, 80134, Napoli, Italy.
Luciano
L
Pirone
Dipartimento di Farmacia, Università di Napoli federico II, Via D. Montesano 49, 80131, Napoli, Italy.
Luciano
L
Mayol
Istituto di Biostrutture e Bioimmagini, CNR, Via Mezzocannone 16, 80134, Napoli, Italy.
Emilia
E
Pedone
Dipartimento di Farmacia, Università di Napoli federico II, Via D. Montesano 49, 80131, Napoli, Italy.
Antonella
A
Virgilio
Dipartimento di Farmacia, Università di Napoli federico II, Via D. Montesano 49, 80131, Napoli, Italy.
Aldo
A
Galeone
D052157:Aptamers, Nucleotide / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D001483:Base Sequence; D054856:G-Quadruplexes; D019427:HIV Integrase / Q000378:metabolism*; D011485:Protein Binding
D052157:Aptamers, Nucleotide; D019427:HIV Integrase; C514801:p31 integrase protein, Human immunodeficiency virus 1
Aptamer T30695; Circular dichroism; G-quadruplex; HIV-1 integrase; Microscale thermophoresis; NMR