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Flouorescence spectrometric study of interaction between complex [Cu(Glu·Arg)]SO_4·5H_2O and bovine serum albumin

Yin Lin-b

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Abstract

The binding interaction between the mixed complexes([Cu(Glu·Arg) ]SO4·5H2O) and bovine serum albumin(BSA) was investigated by fluorescence spectroscopy.The mixed complexes was designed and synthesized with Cu(Ⅱ),glutamate(Glu) and arginine(Arg).The mixed complexes have powerful ability to quench the BSA fluorescence via a static quenching mechanism and quenching rate constant is1.2 × 1012L·mol- 1·s- 1and binding constant is 9.7 × 103L/mol and the number of binding site is 0.966.

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What this paper is about

The binding interaction between the mixed complexes([Cu(Glu·Arg) ]SO4·5H2O) and bovine serum albumin(BSA) was investigated by fluorescence spectroscopy.The mixed complexes was designed and synthesized with Cu(Ⅱ),glutamate(Glu) and arginine(Arg).The mixed complexes have powerful ability to quench the BSA fluorescence via a static quenching mechanism and quenching rate constant is1.2 × 1012L·mol- 1·s- 1and binding constant is 9.7 × 103L/mol and the number of binding site is 0.966.

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Available abstract

The binding interaction between the mixed complexes([Cu(Glu·Arg) ]SO4·5H2O) and bovine serum albumin(BSA) was investigated by fluorescence spectroscopy.The mixed complexes was designed and synthesized with Cu(Ⅱ),glutamate(Glu) and arginine(Arg).The mixed complexes have powerful ability to quench the BSA fluorescence via a static quenching mechanism and quenching rate constant is1.2 × 1012L·mol- 1·s- 1and binding constant is 9.7 × 103L/mol and the number of binding site is 0.966.

Key concepts: Chemistry, Bovine serum albumin, Binding constant, Quenching (fluorescence), Fluorescence spectroscopy, Arginine, Fluorescence, Binding site

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