Spectroscopic Studies on Interaction Between 3-Bromopyruvic Acid and Human Serum Albumin
The interaction between 3-bromopyruvic acid(3-BrPA) and human serum albumin was studied using fluorescence spectroscopy,synchronous fluorescence spectra,UV/Vis and circular dichroism spectra.Static quenching was predominant between 3-BrPA and HSA,and non-radiation energy transfer between molecules was observed.The results showed that electrostatic force played an important role in the binding reaction.Synchronous fluorescence spectral results revealed that the binding of 3-BrPA induced conformational changes of tyrosine and tryptophan of HSA.3-BrPA mainly interacted with the residues surrounding to the tyrosine.The further quenching phenomenon of the interaction between 3-BrPA and HSA induced by Zn2+ was investigated with the application of fluorescence spectroscopy.The secondary structure of HSA was studied with the presence of 3-BrPA using CD spectra and the result proved that 3-BrPA had little influence on HSA.