Abstract
In this paper we have studied peculiarities of protein-ligand interaction under different conditions. We have shown that guanidine hydrochloride (GdnHCI) 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-day 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.
Highlights
Construction of biosensor system for noninvasive permanent monitoring of glucose level in the human blood is of high importance for diabetic patients [1, 2]
One of the most promising directions for persistent glucose monitoring is the design and development of biosensor systems in which glucose binds to proteins acting as the sensitive element [3]
galactose/D-glucose-binding protein (GGBP) has a low dissociation constant of glucose binding (1 μM) meaning that it can be used as a sensitive element of Spectroscopy: An International Journal biosensor systems in which sampling of blood or interstitial liquid is associated with dilution
Summary
Construction of biosensor system for noninvasive permanent monitoring of glucose level in the human blood is of high importance for diabetic patients [1, 2]. One of the most promising directions for persistent glucose monitoring is the design and development of biosensor systems in which glucose binds to proteins acting as the sensitive element [3]. D-galactose/D-glucose-binding protein (GGBP) can be used as a sensing element of such biosensor system as the interaction between GGBP and glucose results in a significant conformational change of the protein structure [4]. GGBP has a low dissociation constant of glucose binding (1 μM) meaning that it can be used as a sensitive element of Spectroscopy: An International Journal biosensor systems in which sampling of blood or interstitial liquid is associated with dilution. An important and desirable feature of any biosensor system is the stability of its sensitive element under different denaturing conditions. An essential influence of viscosity of solution on protein-ligand interaction has been observed
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