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A novel copper(Ⅱ) complex with the reduced Schiff base, [Cu(L)_2]·H_2O(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 P212121, with a = 8.9040(18), b = 9.1530(18), c = 24.891(5) ?, V = 2028.6(7) ?3, Z = 4, C_(20)H_(26) Cu N_2O_9, Mr = 501.97, Dc = 1.644g·cm3, μ = 1.135 mm-1, F(000) = 1044, GOOF = 1.194, the final R = 0.0484 and w R = 0.1420 for 6186 observed reflections(I > 2σ(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 μM) and TCPTP(IC50, 0.57 μM) with a moderate selectivity.
A novel copper (Ⅱ) complex with the reduced Schiff base, [Cu (L) _2] · H_2O (I, HL = N- (4- hydroxybenzyl) -L-serine) was prepared in aqueous solution and characterized by elemental analysis Complex I crystallizes in the orthorhombic system, space group P212121, with a = 8.9040 (18), b = 9.1530 (18), c = 24.891 (5), FT-IR, electrospray ionization mass spectrometry and single- , V = 2028.6 (7)? 3, Z = 4, C 20 H 26 Cu N 2 O 9, Mr = 501.97, Dc = 1.644 g cm 3, μ = 1.135 mm -1, F 000 = 1044, GOOF = 1.194, the final R = 0.0484 and w R = 0.1420 for 6186 observed reflections (I> 2σ (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 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 μM) and TCPTP (IC50, 0.57 μM) with a moderate selectivity.