Protein-ligand interactions of the D-galactose/D-glucose-binding protein as a potential sensing probe of glucose biosensors

Olga V. Stepanenko, Olesya V. Stepanenko, Alexander V. Fonin, Vladislav V. Verkhusha, Irina M. Kuznetsova, Konstantin K. Turoverov

Research output: Chapter in Book/Report/Conference proceedingChapter


In this work we have studied peculiarities of protein-ligand interaction under different conditions. We have shown that guanidine hydrochloride (GdnHCl) unfolding-refolding of GGBP in the presence of glucose (Glc) is reversible, but the equilibrium curves of complex refolding-unfolding have been attained only after 10 days incubation of GGBP/Glc in the presence of GdnHCl. This effect has not been revealed at heat-induced GGBP/Glc denaturation. Slow equilibration between the native protein in GGBP/Glc complex and the unfolded state of protein in the GdnHCl presence is connected with increased viscosity of solution at moderate and high GdnHCl concentrations which interferes with diffusion of glucose molecules. Thus, the limiting step of the unfolding-refolding process of the complex GGBP/Glc is the disruption/tuning of the configuration fit between the protein in the native state and the ligand.

Original languageEnglish (US)
Title of host publicationSpectroscopy of Biological Molecules. Proceedings from the 14th European Conference on the Spectroscopy of Biological Molecules 2011
EditorsMaria Marques, Luis Batista de Carvalho, Parvez Haris
Number of pages6
StatePublished - Nov 27 2013

Publication series

NameAdvances in Biomedical Spectroscopy
ISSN (Print)1875-0656


  • D-galactose/D-glucose-binding protein
  • biosensor system
  • intrinsic fluorescence of proteins
  • protein stability
  • viscosity

ASJC Scopus subject areas

  • Radiology Nuclear Medicine and imaging


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