An anti-HIV peptide, T22, forms a highly active complex with Zn(II)

Biochemical and Biophysical Research Communications
H TamamuraN Fujii

Abstract

T22 ([Tyr5,12, Lys7]-polyphemusin II) has been shown to have strong anti-human immunodeficiency virus (HIV) activity, comparable to that of 3'-azide-2', 3'-dideoxythymidine (AZT). T22 takes an antiparallel beta-sheet structure maintained by two disulfide bridges and contains two antiparallel repeats of Cys-Tyr-Arg-Lys-Cys. As reported herein, fully reduced T22 was found by HPLC and ion spray mass spectrometric analyses to form a complex in a molar ratio of 1:1 with Zn(II) ion at neutral pH in aqueous solution. Complexation of Zn(II) ion to this peptide appears to result in tetracoordinate bonding to sulfur atoms of four Cys residues. We also found that the anti-HIV activity of the T22-Zn(II) complex was fourfold stronger than that of T22.

Citations

Mar 19, 1999·AIDS Research and Human Retroviruses·N SeddikiA G Hovanessian
Aug 13, 2009·Journal of Peptide Science : an Official Publication of the European Peptide Society·Nami OhashiHirokazu Tamamura
Jul 16, 2008·Chemical Biology & Drug Design·Xiangyang Liang
Dec 14, 2007·Expert Opinion on Therapeutic Targets·Ye Che, Garland R Marshall
May 20, 1999·Biopolymers·D Andreu, L Rivas
Jan 5, 2002·Biopolymers·G R Marshall
May 31, 2007·Chemical Society Reviews·Xiangyang LiangPeter J Sadler
Apr 21, 2012·Organic & Biomolecular Chemistry·Shinya Oishi, Nobutaka Fujii
Oct 27, 2001·Journal of Natural Products·B R O'Keefe

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