Institute of Molecular Science, Key Laboratory of Chemical Biology and Molecular Engineering of the Education Ministry, Shanxi University, Taiyuan, Shanxi 030006, PR China.
Dalton Trans. 2011 Jun 28;40(24):6532-40. doi: 10.1039/c1dt10169b. Epub 2011 May 24.
Six copper complexes of Schiff base ligands containing 3,5-substituted-4-salicylideneamino-3,5-dimethyl-1,2,4-triazole have been synthesized and well characterized. The structures of complexes 1 and 2 were determined by X-ray crystal analysis. Fluorescence and potentiometric study indicated that in the physiological pH range, one ligand was dissociated from the complexes to form 1:1 mononucleus copper complexes. The complexes potently inhibit protein tyrosine phosphatase 1B (PTP1B), T-cell protein tyrosine phosphatase (TCPTP), megakaryocyte protein tyrosine phosphatase 2 (PTP-MEG2) and Src homology phosphatase 1 (SHP-1) with 3-4 fold selectivity against PTP1B over TCPTP and PTP-MEG2, and 3-9 fold over SHP-1, but display almost no inhibition against Src homology phosphatase 2 (SHP-2). Complex 1 inhibits PTP1B with a competitive model with K(i) of 30 nM. Substitution with small groups at the phenyl of the ligand does not obviously influence the inhibitory ability of the complexes.
六种含 3,5-取代-4-水杨醛亚胺基-3,5-二甲基-1,2,4-三唑的席夫碱配体的铜配合物已被合成并得到很好的表征。配合物 1 和 2 的结构通过 X 射线晶体分析确定。荧光和电位研究表明，在生理 pH 范围内，一个配体从配合物中解离出来形成 1:1 单核铜配合物。这些配合物对蛋白酪氨酸磷酸酶 1B（PTP1B）、T 细胞蛋白酪氨酸磷酸酶（TCPTP）、巨核细胞蛋白酪氨酸磷酸酶 2（PTP-MEG2）和Src 同源磷酸酶 1（SHP-1）具有很强的抑制作用，对 PTP1B 的选择性是 TCPTP 和 PTP-MEG2 的 3-4 倍，是 SHP-1 的 3-9 倍，但对 Src 同源磷酸酶 2（SHP-2）几乎没有抑制作用。配合物 1 以竞争性模式抑制 PTP1B，K(i)为 30 nM。配体苯环上的小基团取代不会明显影响配合物的抑制能力。
