Studies on the Interaction Between Evansblue and Bovine Serum Albumin by Fluorescence Spectrophotometry
Li Ma
Abstract
Li Ma
Abstract
The interaction of evansblue(EB) and bovine serum albumin(BSA)was studied by fluorescence spectroscopy and ultraviolet spectroscopy.The experimental results showed that EB could quench the inner fluorescence of BSA by forming the BSA-EB complex.It was found that both static quenching and non-radiation energy transfer led to the fluorescence quenching.The binding constants(K)between EB and BSA were 1.122×106L·mol-1,and the binding sites(n) were 0.994.According to Foerster theory of non-radiation energy transfer the binding distance(r=3.14nm) and the efficiency of energy transfer(E=0.276) were also obtained.The effect of EB on the conformational change of BSA was also analyzed by synchronous fluorescence spectroscopy.
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The interaction of evansblue(EB) and bovine serum albumin(BSA)was studied by fluorescence spectroscopy and ultraviolet spectroscopy.The experimental results showed that EB could quench the inner fluorescence of BSA by forming the BSA-EB complex.It was found that both static quenching and non-radiation energy transfer led to the fluorescence quenching.The binding constants(K)between EB and BSA were 1.122×106L·mol-1,and the binding sites(n) were 0.994.According to Foerster theory of non-radiation energy transfer the binding distance(r=3.14nm) and the efficiency of energy transfer(E=0.276) were also obtained.The effect of EB on the conformational change of BSA was also analyzed by synchronous fluorescence spectroscopy.
Key concepts: Bovine serum albumin, Fluorescence, Chemistry, Quenching (fluorescence), Fluorescence spectroscopy, Spectroscopy, Ultraviolet visible spectroscopy, Analytical Chemistry (journal)