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
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
收藏
页码:19 / 22
页数:4
相关论文
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[21]   The abasic site lesions in the human telomeric sequence d[TA(G3T2A)3G3]: A thermodynamic point of view [J].
Virgilio, Antonella ;
Petraccone, Luigi ;
Esposito, Veronica ;
Citarella, Giuseppe ;
Giancola, Concetta ;
Galeone, Aldo .
BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS, 2012, 1820 (12) :2037-2043