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2013•Journal of Zhejiang International Studies UniversityRequires access

The Influence of Ionic Strength on the Interaction of N-Tetradecyl-N-Hydroxyethyl-N,N-Dimethyl Ammonium Bromide and Bovine Serum Albumins

Shen Yingyin

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Abstract

The interaction of N-tetradecyl-N-hydroxyethyl-N,N-dimethyl ammonium bromide and bovine serum albumins in Tris-HCl buffer solution( pH = 7. 1) under different ionic strength was studied by fluorescence spectroscopy at 298 K. The influence of inonic strength on the interaction between THDAB and BSA within a relatively low concentration range was examined. The interaction mechanism between THDAB and BSA at a relatively low concentration range was discussed using the Stern-Volmer equation. The binding constant and the number of binding site of the binding reaction between THDAB and BSA under different ionic strength were calculated using site binding model. Result indicated that along with the enhancement of ionic strength,the interaction of THDAB and BSA was weakened.

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What this paper is about

The interaction of N-tetradecyl-N-hydroxyethyl-N,N-dimethyl ammonium bromide and bovine serum albumins in Tris-HCl buffer solution( pH = 7. 1) under different ionic strength was studied by fluorescence spectroscopy at 298 K. The influence of inonic strength on the interaction between THDAB and BSA within a relatively low concentration range was examined. The interaction mechanism between THDAB and BSA at a relatively low concentration range was discussed using the Stern-Volmer equation. The binding constant and the number of binding site of the binding reaction between THDAB and BSA under different ionic strength were calculated using site binding model. Result indicated that along with the enhancement of ionic strength,the interaction of THDAB and BSA was weakened.

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Available abstract

The interaction of N-tetradecyl-N-hydroxyethyl-N,N-dimethyl ammonium bromide and bovine serum albumins in Tris-HCl buffer solution( pH = 7. 1) under different ionic strength was studied by fluorescence spectroscopy at 298 K. The influence of inonic strength on the interaction between THDAB and BSA within a relatively low concentration range was examined. The interaction mechanism between THDAB and BSA at a relatively low concentration range was discussed using the Stern-Volmer equation. The binding constant and the number of binding site of the binding reaction between THDAB and BSA under different ionic strength were calculated using site binding model. Result indicated that along with the enhancement of ionic strength,the interaction of THDAB and BSA was weakened.

Key concepts: Ionic strength, Ammonium bromide, Chemistry, Bovine serum albumin, Bromide, Ammonium, Fluorescence spectroscopy, Binding constant

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The Influence of Ionic Strength on the Interaction of N-Tetradecyl-N-Hydroxyethyl-N,N-Dimethyl Ammonium Bromide and Bovine Serum Albumins — Research Paper | ScholarLens