Studys On The Synthesis,Characterization And The Interaction Of Transition Metal Complex Of Rutin With Serum Albumin

Protein plays an important part in life process. Serum albumin is a kind of protein which can bind with intrinsic and extrinsic materials, and transfer them to every parts of the body. Therefore, the study of the interaction between small molecules and Bovine serum albumin(BSA) and Human serum albumin(HSA) is a very important task in the fields of life science and chemistry.Rutin has many physiological activities. It can maintain the resistance of the blood vessel, reduce their osmoses and brittleness, promote proliferation of the cells and prevent the blood cells from agglutination. In addition, rutin has many other functions, such as anti-inflammatory, antiallergic, diuretic, spasmolytic, reducing blood-fat, cardiotonic, protecting ulcer surfaces, etc. Therefore it has been used in clinical treatment. At the same time, transition metal complexes have become a intersectant subject and foreland field for their special properties such as characterizations in light, electricity, magnetism, catalysis and biochemistry. The nitrogen complexes have been applied diffusely in synthesis and research of transition metal complexes for their better cooperation capability. In this dissertation, four kinds of complexes were synthesized with the microelement such as Ni(II),Co(II),Cu(II) and Cd(II) in body as center ions, and the ligand rutin—a flavonoids antibiotic and has been extensively used in the clinic medicine .The complexes have been characterized by IR spectrum, UV spectrum and elemental analysis diffraction, and the general formula of this complexes, ML₂HCO₃Na·nH₂O (M=Cu,Cd, n=l; M=Co, n=6; M=Ni, n=3 ;), is given.Based on this study, interaction between rutin and its complexes and bovine serum albumin (BSA) Human serum albumin (HSA) were studied. The results show that the fluorescence quenching effect of rutin and its complexes on BSA and HSA are because of a Static energy transfer mechanism. The number of binding sites between complexes of rutin and BSA and HSA were deduced to be n_rutin-Cu-BSA=1.6, 1.2; n_rutin-Cu-HSA=1.2, 0.9, and theassociation constant at room temperature was determined to be K_rutin-Cu-BSA=3.4×10⁷(mol/L)^-15.8×10 ⁵(mol/L)^-1; K_rutin-Cu-HSA=1.7×10⁶(mol/L)^-1, 5.0×10⁵ (mol/L)^-1.In addition, the reducing blood pressure behavior of Cd(II)-rutin complex was studied. Results show that rutin-Cd by intravenous injection can reduce blood pressure and rutin-Cdcan decrease tension of aortic smooth muscle string induced by noradrenalin, while treatment with rutin-Cd only has not significant changes of tension of aortic smooth muscle string. Therefore general rutin-Cd can cause decrease of blood pressure and cause relaxation of aortic muscle precontracted by NA.