Study On The Spectral Characteristics Of The Interactions Between Triphenylmethane Acid Dyes And Serum Albumin

Chapter 1: The structure, function and spectrum characteristic of serum albumin and the recent twenty-years research progress on spectrum probes of protein were summarized briefly. Mechanism of the interaction between protein and small molecules and their application were expatiated. The significance and contents of this paper has been presented.Chapter 2: The ultraviolet and fluorescence spectral characteristic of two triphenylmethane acid dyes methyl blue and aniline blue were studied in detail. The spectrographic parameters and fluorescent quantum yield of dyes were determined and the factors that influent luminescence (such as pH value, ionic strength and media condition) were investigated. The results provided the theoretical basic for their application in chemical-biologic analysis and establish of analytic determination.Chapter 3: The interactions between methyl blue and human serum albumin (HSA) were studied by fluorescence spectroscopy. The binding constants and binging sites of methyl blue with HSA were measured at different temperatures. The experimental results revealed that methyl blue has a strong ability to quench the intrinsic fluorescence of HSA and the interaction has been verified as consistent with the static quenching procedure. According thermodynamic parameters, the acting forces were determined to be both hydrophobic force and electrostatic force. Based on the mechanism of the Forster energy transference, the transfer efficiency of energy E and transfer distance r between the acceptor methyl blue and HSA were obtained. E was 0.63 and r was 2.06.Chapter 4: The interactions between aniline blue and human serum albumin (HSA) were studied by fluorescence spectroscopy. The binding constants and binging sites of aniline blue with HSA were measured at different temperatures. The experimental results revealed that aniline blue...