N-(2-吡啶甲基)-L-丝氨酸铜配合物的合成、晶体结构及抑制蛋白酪氨酸磷酸酶活性

在甲醇溶液中, 还原希夫碱HLN-(2-吡啶甲基)-L-丝氨酸]与CuCl₂·2H₂O以摩尔比1∶1反应, 得到1个新的中性单核铜配合物CuLCl(H₂O)](Ⅰ). 通过X射线单晶衍射、 元素分析、 红外光谱、 电喷雾质谱和粉末X射线衍射分析等对其进行了表征. 晶体结构分析表明, 在该配合物中还原希夫碱以三齿双螯合环配位到中心铜离子, 同时氯离子和溶剂水分子也参与配位, 形成1个具有四方锥构型的五配位铜(Ⅱ)配合物, 该配合物通过分子间弱相互作用连接成二维超分子结构. 生物活性测试结果表明, 配合物Ⅰ能有效抑制蛋白酪氨酸磷酸酶1B(PTP1B)和T细胞蛋白酪氨酸磷酸酶(TCPTP), IC₅₀值分别为0.32和0.45 μmol/L.

Synthesis,Crystal Structure and Protein Tyrosine Phosphatase Inhibition of a Copper(Ⅱ) Complex with N-(2-Pyridylmethyl)-L-serine†

The reaction of the reduced Schiff base HL N-(2-pyridylmethyl)-L-serine] with CuCl₂·2H₂O in molar ratio of 1∶1 in methanol solution afforded a new neutral mononuclear complex CuLCl(H₂O)](Ⅰ). The structure was determined by single-crystal X-ray diffraction and further characterized by elemental analysis, FTIR, electrospray ionization mass spectrometry and powder X-ray diffraction. In complex Ⅰ, the Cu(Ⅱ) ion adopts five-coordinated mode in a square pyramidal configuration which is completed by one oxygen and two nitrogen atoms from the L^- anion, one chloride anion and one water molecule. The discrete copper coordination units were extended into a 2D supramolecular network through the intermolecular interactions. The bioactivity of the compound as a potential PTPs(Protein Tyrosine Phosphatases) inhibitory agent in vitro was investigated, displaying potent inhibition against PTP1B(IC₅₀=0.32 μmol/L) and TCPTP(IC₅₀=0.45 μmol/L).