一种抗HIV肽T22与锌（II）形成一种高活性复合物。
An anti-HIV peptide, T22, forms a highly active complex with Zn(II).
作者信息
Tamamura H, Otaka A, Murakami T, Ibuka T, Sakano K, Waki M, Matsumoto A, Yamamoto N, Fujii N
机构信息
Faculty of Pharmaceutical Sciences, Kyoto University, Japan.
出版信息
Biochem Biophys Res Commun. 1996 Dec 13;229(2):648-52. doi: 10.1006/bbrc.1996.1858.
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.
T22（[酪氨酸5,12，赖氨酸7] - 海胆精蛋白II）已被证明具有强大的抗人类免疫缺陷病毒（HIV）活性，与3'-叠氮-2'，3'-双脱氧胸苷（AZT）相当。T22具有由两个二硫键维持的反平行β-折叠结构，并包含两个Cys-Tyr-Arg-Lys-Cys的反平行重复序列。如本文所报道，通过高效液相色谱（HPLC）和离子喷雾质谱分析发现，在中性pH的水溶液中，完全还原型的T22与锌（II）离子以1:1的摩尔比形成复合物。锌（II）离子与该肽的络合似乎导致与四个半胱氨酸残基的硫原子形成四配位键。我们还发现，T22-锌（II）复合物的抗HIV活性比T22强四倍。
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