Research Article Open Access

Binding Interaction between Bovine Serum Albumin and Chicoric Acid, a Food Functional Component

Haifang Xiao1, Quancai Sun2, Xuebo Liu2 and Yuanda Song1
  • 1 Shandong University of Technology, China
  • 2 Northwest A&F University, China

Abstract

Fuorescence, FTIR and UV-Vis absorption spectroscopy were used to explore the binding between chicoric acid and Bovine Serum Albumin (BSA). Binding characteristics at various levels of temperature have been calculated. The results indicated that chicoric acid statically quenched the intrinsic fluorescence of BSA. The binding constants (Ka) were 4.14×105 L mol-1 at 273K and 4.29×106 L mol-1 at 298 k. The numbers of binding sites between chicoric acid and BSA were both approximately equal to 1 at the two temperatures. Furthermore, the binding distance between chicoric acid and BSA was 2.69 nm which was calculated according to the Förster’s resonance energy transfer. Thermodynamic parameters suggested that BSA bind chicoric acid spontaneously mainly via hydrophobic interaction. Results demonstrated that the conformation and microenvironment of BSA were changed after binding with chicoric acid. Moreover, chicoric acid showed stronger binding with tryptophan (Trp) residue than with tyrosine (Tyr) residue. Our results can provide scientific basis for studying availability and distribution of chicoric acid.

American Journal of Biochemistry and Biotechnology
Volume 12 No. 3, 2016, 149-158

DOI: https://doi.org/10.3844/ajbbsp.2016.149.158

Submitted On: 26 May 2016 Published On: 19 September 2016

How to Cite: Xiao, H., Sun, Q., Liu, X. & Song, Y. (2016). Binding Interaction between Bovine Serum Albumin and Chicoric Acid, a Food Functional Component. American Journal of Biochemistry and Biotechnology, 12(3), 149-158. https://doi.org/10.3844/ajbbsp.2016.149.158

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Keywords

  • Chicoric Acid Bovine Serum Albumin
  • Spectroscopy
  • Interaction
  • Conformation