Exploring the binding of d(GGGT)4 to the HIV-1 integrase: An approach to investigate G-quadruplex aptamer/target protein interactions

被引：21

作者：

Esposito, Veronica ^{[1
]}

Pirone, Luciano ^{[2
]}

Mayol, Luciano ^{[1
]}

Pedone, Emilia ^{[2
]}

Virgilio, Antonella ^{[1
]}

Galeone, Aldo ^{[1
]}

机构：

[1] Univ Naples Federico II, Dipartimento Farm, Via D Montesano 49, I-80131 Naples, Italy

[2] CNR, Ist Biostrutture & Bioimmagini, Via Mezzocannone 16, I-80134 Naples, Italy

来源：

BIOCHIMIE | 2016年 / 127卷

关键词：

Aptamer T30695; G-quadruplex; HIV-1; integrase; Microscale thermophoresis; Circular dichroism; NMR; TETRAD-FORMING OLIGONUCLEOTIDES; ANTI-HIV; INHIBITOR; STACKING; DOMAINS;

D O I：

10.1016/j.biochi.2016.04.013

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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. (C) 2016 Elsevier B.V. and Societe Francaise de Biochimie et Biologie Moleculaire (SFBBM). All rights reserved.

引用

页码：19 / 22

页数：4

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