Study On The Interaction Between Several Metal Complexes And Serum Albumin

Cerebral thrombosis become a common disease in the elderly,because human society is going to a aging society. Serum albumin which is a major component of plasma can combine with a number of endogenous and exogenous substances and transport these substances to various organs of the body. So, person start to pay attention of serum proteins in thrombus formation in the biological mechanism. In this paper, using UV absorption spectroscopy, fluorescence spectroscopy, circular dichroism method and other methods to discuss the interaction between serum albumin and metal complexes of anticoagulant function. Hoping to provide some of the reference for synthetic good anti-clotting effect, low toxicity, water-soluble drugs.This paper consists of four parts:PARTâ… : Introduction serum albumin's composition, structural characteristics, physiological functions and its spectral properties briefly. Some introductions for methodology of the interaction between small molecules and HSA was discrebed. This article used fluorescence spectroscopy carried out a more detailed description.PARTâ…¡: The interaction between bovine serum albumin and metal complexes of salicylic acid has been studied by fluorescence spectroscopy. It was observed that metal complexes of salicylic acid could reduce the fluorescence intensity of bovine serum albumin. The way of fluorescence quenching was static quenching, and the binding constant and binding sites was calculated. And using the circular dichroism method to study the impact of salicylic acid metal complexes on the secondary structure of bovine serum albumin, and founding that salicylic acid metal complexes has obviously changed the conformation of bovine serum albumin.PARTâ…¢: The interactions between the anti-clotting effect of transition metals iron and copper warfarin, salicylic acid ternary complex and Human Serum Albumin was researched by fluorometry. Finding iron, copper ternary complex could reduce the fluorescence intensity of human serum albumin. The way of fluorescence quenching was static quenching, and the binding constant and binding sites was calculated. According to the thermodynamic functions at different temperatures, it can be identify the force type of complexes with human serum albumin. The existence of ternary complexes significant changed the conformation of human serum albumin, and the reasons for changing the conformational of HSA by complexes was discussed.PARTâ…£: Some research work has been done for the interaction between HSA and neodymium complexes which has anti-clotting effect by fluorescence, UV spectroscopy and circular dichroism method. The results showed that: the interaction between HSA with warfarin neodymium and warfarin salicylate neodymium complexes which have anti-coagulant effect belonged to the static quenching effect because of the non-fluorescent compound generated. The quenching of salicylic neodymium contains dynamic quenching and static quenching. It could be identify the force type of complexes with human serum albumin. The main forces between warfare neodymium and HSA is the electrostatic force; The main force between Salicylate neodymium and HSA is typical hydrophobic force; The main force between warfare acid neodymium and HSA is hydrogen bonding and van der Waals forces. The binding constant K and the binding sites n of complexes with HSA was gained.