Drug Molecules Interact With Serum Albumin Fluorescence Spectroscopy Study

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. Fluorescence spectrum is an extensively used technology in protein analysis. The study of the interaction between small organic molecules especially drugs and serum albumin is distinctively important in the clinic medicine and life science.In this thesis, we studied the interaction between sodium gualenate (SG) and BSA, the fluorescence properties of 5-sulfosalicylic acid (SSA), the interaction between SSA and bovine serum albumin (BSA) and the interaction between SSA and human serum albumin (HSA). Our purpose is to determine the interaction mechanism between small organic molecules and protein. At the same time, the reaction characters between drugs and protein were researched by fluorescence spectrum. The binding parameters (binding constant, binding numbers and the sorts of binding forces et al) were obtained.This thesis includes three parts:1. The interaction between sodium gualenate (SG) and bovine serum albumin (BSA) was studied. The results show the mechanism of quenching belongs to static quenching. The binding numbers and the association constants between SG and BSA were deduced by a new method. According to the thermodynamic parameters, the main sorts of binding force were determined. At last, the effects of five anions on the interaction between SG and BSA were investigated.2. Fluorescence spectra of 5-sulfosalicyclic acid (SSA) were studied.Using quinine bisulphate as a reference, fluorescence quantum yield of SSA was measured. The findings show that SSA is a strong fluorescent material, and its fluorescence quantum is 0.54.3. The interaction between 5-sulfosalicylic acid (SSA) and bovine serum albumin (BSA) was studied by fluorescence spectrum. The results show the mechanism of quenching belongs to static energy transfer quenching and the association constants at different temperature between SSA and BSA were determined. The number of binding sites between SSA and BSA was determined. According to the thermodynamic parameters, the main sorts of binding force were determined. Based on the energy transfer of dipole-dipole interaction between donor and acceptor, the distance between 212-trypyophane residue of BSA and SSA was determined. At last, the effects of several experimental conditions on the interaction were investigated, and the interaction between 5-sulfosalicylic acid (SSA) and human serum albumin (HSA) was studied by fluorescence spectrum.