Studies On The Interactions Between Bovine Serum Albumins And Small Drug Molecules Such As Hydroxybenzene Or Alkaloids Using Spectral Technology

Serum albumin is the most abundant protein in the circulatory system in the body of man or animal, which stores and carries a plenty of drugs to all place of the body, including endogens and exogens, and transfer them to various parts of the body. Therefore, the study of the interaction between serum albumin and drugs is a very important task in the fields of life science and chemistry.Spectroscopy method is of high sensitivity, good selectivity, easy controlling and minimum quantity of used reagent, at the meantime, it can gives the messages of the molecular structure and the changes of molecular conformation. In this paper, the interactions between drugs and bovine serum albumin using fluorescent spectra, synchronous fluorescence, UV-Vis absorption spectra, circular dichroism(CD) spectra, Fourier transformed infrared (FT-IR) spectrometry and Raman spectroscopy were researched,The interaction mechanism,binding constants,thermodynamic binding parameter,separation distance and reaction force between drug small molecules and protein and the effect of the common metal ions on the interactions were studied in detail. It is worth noting that the conclusions obtained from the researches on the interactions between drugs and protein are of great values on biochemistry,pharmaceutical chemistry,clinical medicine and pharmaceutical activity.The mostly approachs and conclusions in this study:(1) The interactions of drugs and bovine serum albumin using UV-Vis absorption spectra were researched. According to the changes of the site and intensity of band of system, it was found that the drug-protein complexes were formed between drug and protein the microenvironment of the tryptophanyl, tyrosine, phenylalanine residues of BSA are change.(2) The interactions of Brerifolin carboxylic acid (BCA), Rosmarinic acid (RA) and bovine serum albumin using fluorescent spectra and synchronous fluorescence spectra were studied. The results showed the mechamism of quenching was to static quenching. The binding sites of the drugs in protein were also discussed, the binding constants of drugs and BSA and the effect of the common metal ions on the interactions were studied in detail. Hydropoblic interaction force played a major in the interaction of BSA with BCA and the interaction of of BSA with RA was Vander walls force. Synchonous fluorescence was used to study protein conformation founded that the polarity of the tyrosine residues was decreased and the hydrophobicity was increased, and in the same time the polarity of the tryptophan residues was increased and the hydrophobicity was decreased.(3) The change ofα-helix after the interaction of the drugs and BSA was investigated using the CD, FT-IR, Raman spectra. The experimental results showed that theα-helix was increased when added to the BRA, MT, OMT. However, the SPR was decreased. And the change of the amide band I, II, III were dicussed in detaid.(4) The studying of the key determining groups were determined according to the inclusions and the structure of these drugs and the effect of the interactions.