Abstract

The interaction of arsenite with a Cys 3His (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 °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.

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