A Copper(II) Complex Based on N-(4-hydroxybenzyl)-L-serine: Synthesis, Crystal Structure and Inhibitory Activity on PTP1B and TCPTP

A novel copper(II) complex with the reduced Schiff base, [Cu(L)(2)]center dot H2O (I, HL = N-(4-hydroxybenzyl)-L-serine), was prepared in aqueous solution and characterized by elemental analysis, FT-IR, electrospray ionization mass spectrometry and single-crystal X-ray diffraction. Complex I crystallizes in the orthorhombic system, space group P2(1)2(1)2(1), with a = 8.9040(18), b = 9.1530(18), c = 24.891(5) angstrom, V = 2028.6(7) angstrom(3), Z = 4, C20H26CuN2O9, M-r = 501.97, D-c = 1.644g.cm(3), mu = 1.135 mm(-1), F(000) = 1044, GOOF = 1.194, the final R = 0.0484 and wR = 0.1420 for 6186 observed reflections (I > 2 sigma(I)). In I, two L- anions are coordinated to the copper ion in tridentate and bidentate chelating modes, respectively, resulting in the coordinated geometry of copper ion to be a distorted square pyramid. The intermolecular hydrogen bonds between the complexes, complexes and lattice water molecules lead to a 2D supramolecular network. The bioactivity of the complex as a potential PTPs inhibitory agent in vitro was investigated, displaying potent inhibition against PTP1B (IC50, 0.27 mu M) and TCPTP (IC50, 0.57 mu M) with a moderate selectivity.