Interaction of arsenite with a zinc finger CCHC peptide: Evidence for formation of an As-Zn-peptide mixed complex

被引:8
作者
Demicheli, Cynthia [1 ]
Frezard, Frederic [2 ]
Pereira, Fernanda A. [1 ]
Santos, Daniel M. [3 ]
Mangrum, John B. [4 ]
Farrell, Nicholas P. [4 ]
机构
[1] Univ Fed Minas Gerais, Dept Quim, Inst Ciencias Exatas, Inst Ciencias Biol, BR-31270901 Belo Horizonte, MG, Brazil
[2] Univ Fed Minas Gerais, Dept Fisiol & Biofis, Inst Ciencias Biol, BR-31270901 Belo Horizonte, MG, Brazil
[3] Univ Fed Minas Gerais, Dept Bioquim Imunol, Inst Ciencias Biol, BR-31270901 Belo Horizonte, MG, Brazil
[4] Virginia Commonwealth Univ, Dept Chem, Richmond, VA 23284 USA
基金
美国国家科学基金会;
关键词
Arsenic; Zinc finger; NCp7; HIV-1 NUCLEOCAPSID PROTEIN; ACUTE PROMYELOCYTIC LEUKEMIA; MOLECULAR-MECHANISM; RAR-ALPHA; PML; TRIOXIDE; BINDING; ACID; TRANSCRIPTION; DEGRADATION;
D O I
10.1016/j.jinorgbio.2011.09.023
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 interaction of arsenite with a Cys(3)His (CCHC) zinc finger model (34-51) HIV-1 nucleocapsid protein p7 (NCp7) peptide in the absence and presence of Zn(II) was studied using fluorescence spectroscopy, CD (circular dichroism) and ESI-MS (Electrospray Ionization Mass Spectrometry). We found that arsenic forms different complexes with the free peptide and the zinc finger peptide. In the former case the peptide conformation differed greatly from that of the zinc finger, whereas in the second case a mixed As-Zn-peptide complex was formed with partial preservation of zinc finger conformation. An apparent stability constant was estimated for the mixed As-Zn-peptide complex (K = 2083 M(-1) and 442 M(-1) at 25 degrees C and pHs 6 and 7, respectively). Our study also shows that the interaction of arsenic with the CCHC motif is facilitated by glutathione (GSH), through formation of a GS-As-peptide conjugate. (C) 2011 Elsevier Inc. All rights reserved.
引用
收藏
页码:1753 / 1758
页数:6
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