Synthesis,Crystal Structure and Bioactivity of a Pd(Ⅱ) Complex with Demethylcantharate and 2,2′-Bipy

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A novel crystal with the molecular formula [Pd(DCA)(bipy)]2 [Pd(bipy)Cl2 ]·6.75H2O was formed by PdCl2 with disodium demethylcantharate (Na2 (DCA),DCA2= 7-oxa-bicyclo[2.2.1]heptane-2,3-bicarboxylate) and 2,2-bipyidine (bipy) through the hydrothermal method.The complex was characterized by elemental analysis and infrared spectroscopy.The structure of the complex was determined by single-crystal X-ray diffraction,which is of triclinic system,space group P1 with a=13.6818(7),b=14.8426(8),c=15.0043(8),α=97.319(3),β=92.521(3),γ=105.776(2)°,V=2898.4(3) 3,Dc=1.545 g·cm-3,Z=1,F(000)=1420,S=0.852,the final R=0.0525 and wR=0.1777 for 13634 observer reflections (I>2σ(I)).The binding reaction of the complex with ct-DNA and bovine serum albumin (BSA) was studied by fluorescence spectroscopy.The results indicated that the complex binds to ct-DNA via the partial intercalation.The binding constant K A of the complex interaction with BSA was 3.98×10 5 L·mol-1 and one binding site would be formed.The antiproliferative activity of the complex against human hepatoma cells (SMMC7721) in vitro is much higher than that of Na 2 (DCA). A novel crystal with the molecular formula [Pd (DCA) (bipy)] 2 [Pd (bipy) Cl2] · 6.75H2O was formed by PdCl2 with disodium demethylcantharate (Na2 (DCA), DCA2 = 7-oxa-bicyclo [2.2. 1] heptane-2,3-bicarboxylate) and 2,2-bipyidine (bipy) through the hydrothermal method. The complex was characterized by elemental analysis and infrared spectroscopy. The structure of the complex was determined by single-crystal X-ray diffraction , which is of triclinic system, space group P1 with a = 13.6818 (7), b = 14.8426 (8), c = 15.0043 (8), α = 97.319 (3), β = 92.521 (3), γ = 105.776 D = 1.545 g-cm-3, Z = 1, F (000) = 1420, S = 0.852, the final R = 0.0525 and wR = 0.1777 for 13634 observer reflections ( I> 2σ (I)). The binding reaction of the complex with ct-DNA and bovine serum albumin (BSA) was studied by fluorescence spectroscopy. These results indicated that the complex binds to ct-DNA via the partial intercalation. The binding constant KA of the complex interaction with BSA was 3.98 × 10 5 L · mol -1 and one binding site would be form ed. the antiproliferative activity of the complex against human hepatoma cells (SMMC7721) in vitro is much higher than that of Na 2 (DCA).
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