Study On The Interaction Of Hemin With Cyclodextrin And Bovine Serum Albumin

In order to improve the defects such as easiness to decompose meeting light or oxygenand poor water-solubility, heimin was included by β-cyclodextrin to form heimin-β-cyclodextrin inclusion. β-cyclodextrin has characteristic structure with hydrophilic outersurface and hydrophobic inner surface and can increase the stability and water-solubility ofother compounds by forming inclusion with them. In this study, microwave method wasemployed to produce inclusion composed of β-cyclodextrin and other compounds. Takeinclusion ratio as object, the process of conclusion was optimized. The inclusion wasidentified through UV and IR spectrometry.The interaction between bovine serum albumin and heimin was investigated byfluorescence spectra and UV. Experimental results indicated that the fluorescence quenchingof heimin to bovine serum albumin was static quenching with the binding sites is1.25and theequilibrium constant K is2.48×10~7L/mol. The binding locality was0.99nm away fromtryptophan residue-212in bovine serum albumin based on F rster’s non-radiation energytransfer mechanism. The effect of heimin on the conformation of bovine serum albumin wasanalyzed by three-dimensional fluorescence spectra, contour spectra and synchronous spectra.The binding of bilirubin to bovine serum albumin was studied using fluorescence spectra.Experimental results indicated that the fluorescence quenching of bilirubin to bovine serumalbumin was static quenching with the binding sites is0.74and equilibrium constant K is4.9×10~4L/mol. The binding locality was2.12nm away from tryptophan residue-212inbovine serum albumin based on F rster’s non-radiation energy transfer mechanism. Theeffect of bilirubin on the conformation of bovine serum albumin was analyzed byfluorescence spectra.