Journal of Solution Chemistry

, Volume 45, Issue 2, pp 265–285 | Cite as

Influence of Taxifolin on the Human Serum Albumin–Propranolol Interaction: Multiple Spectroscopic and Chemometrics Investigations and Molecular Dynamics Simulation

  • Fatemeh Sadat Mohseni-Shahri
  • Mohammad Reza Housaindokht
  • Mohammad Reza Bozorgmehr
  • Ali Akbar Moosavi-Movahedi
Article
First Online:
Received:
Accepted:

Abstract

The aim of the present study is to characterize the competition between propranolol (PROP) and taxifolin (TAX) in binding to human serum albumin (HSA) in a physiological buffer (pH 7.4) using multiple spectroscopic, chemometrics and molecular dynamics simulation measurements. Fluorescence analysis was used to determine the binding and quenching properties of HSA–ligand complexes in binary and ternary systems. These spectral data were further analyzed by the multivariate curve resolution-alternating least squares method. In addition, the concentration profiles and pure spectra of three species (HSA, ligand and HSA–ligand complex) and the apparent equilibrium constants K app were evaluated. Fluorescence spectroscopy showed that in the presence of TAX, the binding constant of HSA–PROP increased. The effect of ligands on the secondary structure of the protein has been analyzed by using Fourier transform infrared spectra. The conformational change of the protein was analyzed using synchronous fluorescence spectroscopy, three-dimensional fluorescence spectra and molecular dynamics (MD) simulation. The results of synchronous fluorescence and three-dimensional fluorescence spectra show that PROP alters the microenvironment around the tryptophan (Trp) and tyrosine (Tyr) residues in the presence of TAX. According to the MD simulation, these ligands can interact with the protein, affecting the secondary structure of HSA and modifying its tertiary structure. MD simulations and experimental data support each other.

Keywords

Human serum albumin Falvonoid Chemometrics Conformational change Molecular dynamics simulation 
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Notes

Acknowledgments

The financial support for this work was provided by Research Council of Ferdowsi University of Mashhad (Research Project No. 3/24357-91/10/12).

Supplementary material

10953_2016_435_MOESM1_ESM.doc (1 mb)
Supplementary material 1 (DOC 1027 kb)

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Copyright information

© Springer Science+Business Media New York 2016

Authors and Affiliations

  • Fatemeh Sadat Mohseni-Shahri
    • 1
  • Mohammad Reza Housaindokht
    • 1
  • Mohammad Reza Bozorgmehr
    • 2
  • Ali Akbar Moosavi-Movahedi
    • 3
  1. 1.Department of Chemistry, Faculty of ScienceFerdowsi University of MashhadMashhadIran
  2. 2.Department of Chemistry, Mashhad BranchIslamic Azad UniversityMashhadIran
  3. 3.Institute of Biochemistry and BiophysicsUniversity of TehranTehranIran

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