Study On The Interaction Between Several Anticoagulants And Human Serum Albumin

Nowadays cerebrovascular disease has become the first urban and rural population causes disability and death, and the incidence trend of increasing year by year. Which atherosclerosis-based incidence of ischemic cerebrovascular disease is growing, so anticoagulants for research scientists has long been a focus of the study drugs. But the serum albumin is the most abundant plasma major carrier, it works with many endogenous and exogenous substances with a wide range, the total drug molecules into the body through the storage and transport of plasma to reach the receptor site occurs pharmacological effect, while serum albumin is also a component of thrombosis. Therefore, the study drugs and the role of serum albumin has important significance. In this paper, using fluorescence spectroscopy, UV absorption spectroscopy, Circular Dichroism(CD) method and other methods to discuss the interaction between human serum albumin(HSA) 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…¡: Fluorescence spectroscopy, UV spectra and Circular Dichroism are applied to study interaction between human serum albumin and anticoagulants warfarin at different temperatures. The quenching mechanism of fluorescence of HSA by warfarin is found to be a static quenching procedure and the binding constant K and binding sites n are calculated. According to the thermodynamic functions at different temperatures, the binding type of warfarin to HSA is hydrongen bond and van der Waals force. The research results shown that the precense of warfarin can cause a change of the human serum albumin conformation, and the reasons for the change have been discussed. PARTâ…¢: Fluorescence and UV spectra were used to study the interaction between human serum albumin and transition metals iron warfarin binary complexes with anti-cruor function. It was observed that complexes can reduce the fluorescence intensity of human serum albumin. The way of fluorescence quenching was static quenching, and then calculated the binding constant K (about 106) and binding sites n(>1). According to the thermodynamic functions at different temperatures, the binding type of complexes to HSA is hydrongen bond and van der waals. And found that complexes have obviously changed the conformation of human serum albumin. The possible reason for which the complex makes serum albumin conformation changes is discussed.At the same time, the possible reason that interaction between transition metals iron warfarin complexes and human serum albumin is stronger than transition metals iron salicylic acid complexes was further explored.PARTâ…£: Fluorescence spectroscopy, UV spectra and Circular Dichroism are applied to study interaction between human serum albumin(HSA) and Salicylate at different temperatures. The quenching mechanism of fluorescence of HSA by salicylate is found to be a static quenching procedure and the binding constant K and binding sites n are calculated. According to the thermodynamic functions at different temperatures, the binding type of Salicylate to HSA is hydrongen bond and van der Waals force. The research results shown that the precense of Salicylate can cause a change of the human serum albumin conformation, and the reasons for the change have been discussed.