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Interaction Between 1,10-Phenanthroline Aminoacidato Copper(II) Complexes and Bovine Serum Albumin

Xue‐Yi Le

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Abstract

The binding interaction between the complexes,ClO4(1)(L-Phe=L-phenylalanine, ClO4·2.5H2O(2)(Gly =glycine) and bovine serum albumin(BSA) was investigated by fluorescence spectroscopy technique.The results showed that the fluorescence strength of BSA decreased with the increase of the complex concentration,and the binding constant K for complex(2) is bigger than that for complex(1),and the binding site number of BSA to the complexes is 1.

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What this paper is about

The binding interaction between the complexes,ClO4(1)(L-Phe=L-phenylalanine, ClO4·2.5H2O(2)(Gly =glycine) and bovine serum albumin(BSA) was investigated by fluorescence spectroscopy technique.The results showed that the fluorescence strength of BSA decreased with the increase of the complex concentration,and the binding constant K for complex(2) is bigger than that for complex(1),and the binding site number of BSA to the complexes is 1.

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Available abstract

The binding interaction between the complexes,ClO4(1)(L-Phe=L-phenylalanine, ClO4·2.5H2O(2)(Gly =glycine) and bovine serum albumin(BSA) was investigated by fluorescence spectroscopy technique.The results showed that the fluorescence strength of BSA decreased with the increase of the complex concentration,and the binding constant K for complex(2) is bigger than that for complex(1),and the binding site number of BSA to the complexes is 1.

Key concepts: Bovine serum albumin, Chemistry, Glycine, Copper, Phenanthroline, Binding constant, Fluorescence, Binding site

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