【摘要】 在甲醇溶液中,还原希夫碱HL[N-（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0.45μmol/L.更多还原

【Abstract】 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 [Cu LCl（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).更多还原