NDLI: Greater binding affinity of trivalent antimony to a CCCH zinc finger domain compared to a CCHC domain of kinetoplastid proteins

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Metallomics Vol - 4 Issue - 4

Metallomics Vol - 4 Issue - 3

Metallomics Vol - 4 Issue - 2

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Metallomics Vol -2

Metallomics Vol -1

Greater binding affinity of trivalent antimony to a CCCH zinc finger domain compared to a CCHC domain of kinetoplastid proteins

Content Provider	Royal Society of Chemistry (RSC)
Author	Frézard, Frédéric Silva, Heveline Demicheli, Cynthia Farrell, Nicholas Pimenta, Adriano Monteiro de Castro
Copyright Year	2012
Abstract	It has been reported recently that SbIII competes with ZnII for its binding to the CCHC zinc finger domain of the HIV-1 NCp7 protein, suggesting that zinc finger proteins may be molecular targets for antimony-based drugs. Here, the interaction of SbIII with a CCCH zinc finger domain, which is considered to play a crucial role in the biology of kinetoplastid protozoa, has been characterized for the first time. The binding characteristics of SbIII were compared between a CCCH-type peptide derived from a kinetoplastid protein and two different CCHC-type zinc finger peptides. The formation of 1 : 1 Zn–peptide and Sb–peptide complexes from the different peptides was demonstrated using circular dichroism, UV absorption, fluorescence spectroscopies and ESI-MS. Titration of the Zn–peptide complexes with SbCl3 was performed at pH 6 and 7, exploiting the intrinsic fluorescence of the peptides. The differential spectral characteristics of the peptides allowed for competition experiments between the different peptides for binding of ZnII. The present study establishes that SbIII more effectively displaces ZnII from the CCCH peptide than CCHC ones, as a result of both the greater stability of the Sb–CCCH complex (compared to Sb–CCHC complexes) and the lower stability of the Zn–CCCH complex (compared to Zn–CCHC complexes). Comparison of the binding characteristics of SbIII or ZnII between the CCHC-type peptides with different amino acid sequences supports the model that not only the conserved zinc finger motif, but also the sequence of non-conserved amino acids determines the binding affinity of SbIII and ZnII. These data suggest that the interaction of SbIII with CCCH-type zinc finger proteins may modulate, or even mediate, the pharmacological action of antimonial drugs.
Starting Page	433
Ending Page	440
Page Count	8
File Format	HTM / HTML PDF
ISSN	17565901
Volume Number	4
Issue Number	5
Journal	Metallomics
DOI	10.1039/c2mt00176d
Language	English
Publisher	Royal Society of Chemistry
Access Restriction	Open
Subject Keyword	Kinetoplastida Protozoa CCHC Fluorescence Protein Circular dichroism Subtypes of HIV Zinc finger Antimony trichloride PH Titration Molecular biology Peptide
Content Type	Text
Resource Type	Article
Subject	Chemistry Medicine Metals and Alloys Biochemistry Biomaterials Biophysics

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