D-Galactose/D-glucose-binding protein from E. coli (GGBP) is a monomer thatbinds glucose with high affinity. The protein structure of GGBP is organized in twoprincipal domains linked by a hinge region that form the sugar-binding site. In this workwe show that the mutant form of GGBP at the amino acid position 182 can be utilized as aprobe for the development of a non-consuming analyte fluorescence biosensor to monitorthe glucose level in diabetes health care.
Download full-text PDF |
Source |
---|---|
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3864534 | PMC |
http://dx.doi.org/10.3390/s7102484 | DOI Listing |
J Chem Inf Model
February 2021
Department of Chemistry, Multiscale Research Institute of Complex Systems and Institute of Biomedical Sciences, Fudan University, Shanghai 200438, China.
The d-glucose/d-galactose-binding protein (GGBP) from is a substrate-binding protein (SBP) associated with sugar transport and chemotaxis. It is also a calcium-binding protein, which makes it unique in the SBP family. However, the functional importance of Ca binding is not fully understood.
View Article and Find Full Text PDFJ Fluoresc
January 2015
Institute of Cytology of the Russian Academy of Sciences, Tikhoretsky ave., 4, 194064, St. Petersburg, Russia.
Changes of the characteristics of intrinsic tryptophan fluorescence of the wild type of D-galactose/D-glucose-binding protein from Escherichia coli (GGBPwt) induced by D-glucose binding were examined by the intrinsic UV-fluorescence of proteins, circular dyhroism in the near-UV region, and acrylamide-induced fluorescence quenching. The analysis of the different characteristics of GGBPwt and its mutant form GGBP-W183A together with the analysis of the microenvironment of tryptophan residues of GGBPwt revealed that Trp 183, which is directly involved in sugar binding, has the least influence on the provoked by D-glucose blue shift and increase in the intensity of protein intrinsic fluorescence in comparison with other tryptophan residues of GGBP.
View Article and Find Full Text PDFGuang Pu Xue Yu Guang Pu Fen Xi
March 2014
In the glucose measuring technique by surface plasmon resonance, D-galactose/D-glucose binding protein (GGBP) that can specifically adsorb glucose was introduced, and high-precision specific detection of glucose concentration was realized. In the present paper, the GGBP protein was bound on the surface of SPR sensor through thiol coupling method. GGBP binding experiment was carried out on SPR sensor and then glucose concentration experiment was conducted with this sensor.
View Article and Find Full Text PDFJ Phys Chem B
July 2011
Laboratory of Protein structure, stability and folding of proteins, Institute of Cytology RAS, 194064 St. Petersburg, Russia.
The galactose/glucose-binding protein from E. coli (GGBP) is a 32 kDa protein possessing the typical two-domains structure of the ligand-binding proteins family. GGBP is characterized by low dissociation constant values with respect to glucose binding, displaying an affinity constant for glucose in micromolar range.
View Article and Find Full Text PDFJ Phys Chem B
March 2011
Institute of Cytology, Russian Academy of Science, St. Petersburg, Russia.
In this work we have shown that the unfolding-refolding process of the D-galactose/D-glucose-binding protein (GGBP) in the presence of glucose (Glc) induced by the chemical denaturant Gdn-HCI is reversible. In addition, Glc binding does not only stabilize GGBP structure but it also considerably slows down the achievement of the equilibrium between the native protein in GGBP/Glc complex and the unfolded protein. The limiting step of the unfolding-refolding process of the complex GGBP/Glc is the arrangement/de-arrangement of the configuration fit between the protein in the native state and the ligand.
View Article and Find Full Text PDFEnter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!