Direct detection of glucose by surface plasmon resonance with bacterial glucose/galactose-binding protein

Hsieh, Helen; Pfeiffer, Zachary A; Amiss, Terry J.; Sherman, Douglas B.; Pitner, J. Bruce

doi:10.1016/s0956-5663(03)00271-9

Cited by 124 publications

(93 citation statements)

References 31 publications

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“…11,27 Labeling E149C with NBD shows little change from the wild-type GGBP glucose affinity (0.2 µM). Adding L238S to produce E149C/L238S shifts the glucose affinity to 0.080 mM.…”

Section: Discussionmentioning

confidence: 99%

Fluorescence Resonance Energy Transfer Glucose Sensor from Site-Specific Dual Labeling of Glucose/Galactose Binding Protein Using Ligand Protection

Hsieh

Sherman

Andaluz

et al. 2012

J Diabetes Sci Technol

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Background: Site-selective modification of proteins at two separate locations using two different reagents is highly desirable for biosensor applications employing fluorescence resonance energy transfer (FRET), but few strategies are available for such modification. To address this challenge, sequential selective modification of two cysteines in glucose/galactose binding protein (GGBP) was demonstrated using a technique we call "ligand protection." Method: In this technique, two cysteines were introduced in GGBP and one cysteine is rendered inaccessible by the presence of glucose, thus allowing sequential attachment of two different thiol-reactive reagents. The mutant E149C/A213C/L238S was first labeled at E149C in the presence of the ligand glucose. Following dialysis and removal of glucose, the protein was labeled with a second dye, either Texas Red (TR) C5 bromoacetamide or TR C2 maleimide, at the second site, A213C. Results: Changes in glucose-dependent fluorescence were observed that were consistent with FRET between the nitrobenzoxadiazole and TR fluorophores. Comparison of models and spectroscopic properties of the C2 and C5 TR FRET constructs suggests the greater rigidity of the C2 linker provides more efficient FRET. Conclusions: The ligand protection strategy provides a simple method for labeling GGBP with two different fluorophores to construct FRET-based glucose sensors with glucose affinity within the human physiological glucose range (1-30 mM). This general strategy may also have broad utility for other protein-labeling applications.

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“…11,27 Labeling E149C with NBD shows little change from the wild-type GGBP glucose affinity (0.2 µM). Adding L238S to produce E149C/L238S shifts the glucose affinity to 0.080 mM.…”

Section: Discussionmentioning

confidence: 99%

Fluorescence Resonance Energy Transfer Glucose Sensor from Site-Specific Dual Labeling of Glucose/Galactose Binding Protein Using Ligand Protection

Hsieh

Sherman

Andaluz

et al. 2012

J Diabetes Sci Technol

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“…However, a surface-competition assay format was developed that allowed indirect detection of smallmolecule binding (Zhu et al, 2000). Other improvement in SPR instrumentation has enabled detection of small molecules, such as drugs (≥138 Da) binding to human serum albumin (Frostell-Karlsson et al, 2000) and small oligosaccharides (b1000 Da) binding to an antibody (Hsieh et al, 2004). The long-term stability of the surface layer is questionable when in direct contact with blood and the signal is very sensitive to non-specific binding for real-time measurement in blood (Meadows, 1996).…”

Section: Biacore International Ab (Ge Health Care)mentioning

confidence: 99%

Biosensor technology: Technology push versus market pull

Luong

Male

Glennon

2008

Biotechnology Advances

371

178

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“…Glucose/galactose-binding protein (GGBP) is a bacterial periplasmic-binding protein that exhibits a hinge motion and results of conformational change upon binding glucose or galactose molecules [20,21]. Though a lot of research has been done using Glucose/galactose binding protein and its mutation to build biosensor for detecting glucose molecules [22][23][24][25], there is no report on the combination of GBP with BRET to our best knowledge.…”

Section: Introductionmentioning

confidence: 99%

Bioluminescence Resonance Energy Transfer (BRET) Based Nanostructured Biosensor for Tear Glucose Detection

Zhan¹,

Chen²,

Tse³

et al. 2017

International Conference of Theoretical and Applied Nanoscience and Nanotechnology

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-The monitoring and management of blood glucose levels are key elements for people with diabetes to maintain their health. Here, we describe a bioluminescence resonance energy transfer (BRET) sensor for non-invasively detecting glucose molecules. The sensor is assembled by conjugating quantum dots CdTe (PL≈ 565nm), which is used as the acceptor, with a recombinant protein containing the bacterial glucose binding protein (GBP), at the N-terminal and a bioluminescent protein Renilla luciferase (Rluc), used as the donor, which is at the C-terminal. The distance between the BRET pair is initially far. In the presence of glucose, GBP binds glucose in a highly specific manner and the conformational change of resultant GBP brings a closer distance between the Rluc and QDs, results an increasing of the emission intensity of the QDs. The bioluminescence intensity of both around 470nm and 565nm are observed. The ratio of the acceptor (QDs) and the donor (Rluc) are also observed to increase with the increasing of the glucose concentration. This study laid a technical foundation for further exploration of non-invasive measurement systems for tear glucose.

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Direct detection of glucose by surface plasmon resonance with bacterial glucose/galactose-binding protein

Cited by 124 publications

References 31 publications

Fluorescence Resonance Energy Transfer Glucose Sensor from Site-Specific Dual Labeling of Glucose/Galactose Binding Protein Using Ligand Protection

Fluorescence Resonance Energy Transfer Glucose Sensor from Site-Specific Dual Labeling of Glucose/Galactose Binding Protein Using Ligand Protection

Biosensor technology: Technology push versus market pull

Bioluminescence Resonance Energy Transfer (BRET) Based Nanostructured Biosensor for Tear Glucose Detection

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