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2009•Journal of Yangtze UniversityRequires access

Studies on the Binding Reaction Features between Neutral Red and Bovine Serum Albumin

Yan Cheng-nong

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Abstract

Under the simulated physiological conditions of animal body and different temperatures,the action of Neutral Red (NR) to bovine serum albumin (BSA) was studied by the fluorescence spectroscopy,three-dimensional fluorescence spectrum,synchronous fluorescence spectrum and ultra-violet spectrum.It is shown that this compound has a quite strong ability to quench the fluorescence launching from BSA,after analyzing and processing the fluorescence quenching data according to Sterm-Volmer equation,Lineweaver-Burk equation and thermodynamic equation,the binding constant and thermodynamic parameters are obtained.The average value of binding constant(KLB:4.250×104KJ·mol-1),thermodynamic parameters(H θ,-6.432 KJ·mol-1,Gθ:-21.38 KJ·mol-1 and Sθ:-48.68J·K-1) and amounts of binding sites(1.155) are obtained in this paper.

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What this paper is about

Under the simulated physiological conditions of animal body and different temperatures,the action of Neutral Red (NR) to bovine serum albumin (BSA) was studied by the fluorescence spectroscopy,three-dimensional fluorescence spectrum,synchronous fluorescence spectrum and ultra-violet spectrum.It is shown that this compound has a quite strong ability to quench the fluorescence launching from BSA,after analyzing and processing the fluorescence quenching data according to Sterm-Volmer equation,Lineweaver-Burk equation and thermodynamic equation,the binding constant and thermodynamic parameters are obtained.The average value of binding constant(KLB:4.250×104KJ·mol-1),thermodynamic parameters(H θ,-6.432 KJ·mol-1,Gθ:-21.38 KJ·mol-1 and Sθ:-48.68J·K-1) and amounts of binding sites(1.155) are obtained in this paper.

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Available abstract

Under the simulated physiological conditions of animal body and different temperatures,the action of Neutral Red (NR) to bovine serum albumin (BSA) was studied by the fluorescence spectroscopy,three-dimensional fluorescence spectrum,synchronous fluorescence spectrum and ultra-violet spectrum.It is shown that this compound has a quite strong ability to quench the fluorescence launching from BSA,after analyzing and processing the fluorescence quenching data according to Sterm-Volmer equation,Lineweaver-Burk equation and thermodynamic equation,the binding constant and thermodynamic parameters are obtained.The average value of binding constant(KLB:4.250×104KJ·mol-1),thermodynamic parameters(H θ,-6.432 KJ·mol-1,Gθ:-21.38 KJ·mol-1 and Sθ:-48.68J·K-1) and amounts of binding sites(1.155) are obtained in this paper.

Key concepts: Fluorescence, Bovine serum albumin, Quenching (fluorescence), Chemistry, Binding constant, Fluorescence spectroscopy, Analytical Chemistry (journal), Spectroscopy

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