Research Article Open Access

Binding Mechanism of Bovine Serum Albumin to Troxerutin by Synchronous Fluorescence Spectroscopy and Chemometrics

Tianhu Wang1, Yi Yan1 and Yinsheng Luo1
  • 1 Jiangsu University of Technology, China

Abstract

Previous works have reported the binding of Bovine Serum Albumin (BSA) to troxerutin by absorption and fluorescence spectroscopy. In order to extend the investigation of their binding characteristics, the study presented here was designed to evaluate their interaction by the synchronous fluorescence spectroscopy and Multivariate Curve Resolution With Alternating Least Squares (MCR-ALS) under simulative physiological conditions. The Evolving Factor Analysis (EFA) and MCR-ALS analysis results show that there are three chemical species in the troxerutin-BSA system, which reveal that the fluorescence quenching of BSA caused by troxerutin may be a static quenching mechanism. The spectral profile of each compound was obtained by the soft of MCR-ALS. The obtained average binding constant is 6.43×105 mol-1 L for BSA and troxerutin concentration ratio is 7 while that is 6.89×105 mol-1 L for troxerutin and BSA concentration ratio is 5. The study might further help us to better understand the structural features and toxicological action of troxerutin at the molecular level.

American Journal of Biochemistry and Biotechnology
Volume 12 No. 2, 2016, 127-132

DOI: https://doi.org/10.3844/ajbbsp.2016.127.132

Submitted On: 17 February 2016 Published On: 14 May 2016

How to Cite: Wang, T., Yan, Y. & Luo, Y. (2016). Binding Mechanism of Bovine Serum Albumin to Troxerutin by Synchronous Fluorescence Spectroscopy and Chemometrics. American Journal of Biochemistry and Biotechnology, 12(2), 127-132. https://doi.org/10.3844/ajbbsp.2016.127.132

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Keywords

  • Bovine Serum Albumin (BSA)
  • Troxerutin
  • Synchronous Fluorescence Spectroscopy
  • MCR-ALS