Exploring binding properties of naringenin with bovine β-lactoglobulin: a fluorescence, molecular docking and molecular dynamics simulation study

Biophys Chem. 2014 Mar-Apr:187-188:33-42. doi: 10.1016/j.bpc.2014.01.003. Epub 2014 Jan 28.

Abstract

In the present study, the binding properties of naringenin (NG) to β-lactoglobulin (BLG) were explored using spectrofluorimetric and molecular modeling techniques. Analysis of spectrofluorimetric titration data represented the formation of 1:1 complex, significant binding affinity, negative values of entropy and enthalpy changes and the essential role of hydrogen bonding and van der Waals interactions in binding of NG to BLG. The value of determined Förster's distance represents the static mechanism for quenching of BLG by NG. The results of fluorescence competitive binding experiments characterize the location of NG binding site in the outer surface of BLG. Molecular docking study showed that NG binds in the outer surface site of BLG which is accompanied with three hydrogen bonds. The support of molecular docking results by biochemical fluorescence experiments confirms the validity of docking calculation. Analysis of molecular dynamics results indicated that NG can interact with BLG without affecting the secondary structure of protein.

Keywords: Binding parameter; Fluorescence quenching; Molecular modeling; Naringenin; β-Lactoglobulin.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Binding Sites
  • Cattle
  • Flavanones / chemistry*
  • Fluorescence*
  • Lactoglobulins / chemistry*
  • Molecular Docking Simulation*
  • Molecular Dynamics Simulation*
  • Molecular Structure

Substances

  • Flavanones
  • Lactoglobulins
  • naringenin