Fluorescence lifetime spectroscopy and imaging of nano-engineered glucose sensor microcapsules based on glucose/galactose-binding protein

Saxl, Tania; Khan, Farhan R.; Matthews, Daniel R.; Zhi, Zheng‐liang; Rolinski, Olaf J.; Ameer-Beg, Simon; Pickup, John C.

doi:10.1016/j.bios.2009.04.003

Cited by 60 publications

(62 citation statements)

References 37 publications

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“…These were found to be 2.7 and 0.9 ns, which from previous work may be considered to correspond respectively to the glucose-bound (closed) and unbound (open) configurations of GBP-Badan. 12 These lifetimes differ only slightly from previously measured values for GBP-Badan in solution, most likely due to the immobilisation of the protein.…”

Section: Ni-nta Agarose Beads For Binding Gbp-badancontrasting

confidence: 53%

“…12,29,30 The binding constant for native GBP is in the micromolar range and therefore unsuitable for clinical glucose monitoring, but we recently reported 30 the synthesis of a new triple mutant of GBP with a K d of 11 mM and operating range of up to 100 mM glucose, which we labelled with the environmentally sensitive fluorophore, Badan, at a position near the binding site. Addition of glucose produced a large increase in both fluorescence intensity and lifetime.…”

Section: 20mentioning

confidence: 99%

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A fluorescence lifetime-based fibre-optic glucose sensor using glucose/galactose-binding protein

Saxl

Khan

Ferla

et al. 2011

Analyst

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This version is available at https://strathprints.strath.ac.uk/30189/ Strathprints is designed to allow users to access the research output of the University of Strathclyde. Unless otherwise explicitly stated on the manuscript, Copyright © and Moral Rights for the papers on this site are retained by the individual authors and/or other copyright owners. Please check the manuscript for details of any other licences that may have been applied. You may not engage in further distribution of the material for any profitmaking activities or any commercial gain. You may freely distribute both the url (https://strathprints.strath.ac.uk/) and the content of this paper for research or private study, educational, or not-for-profit purposes without prior permission or charge.Any correspondence concerning this service should be sent to the Alternative, non-electrochemistry-based technologies for continuous glucose monitoring are needed for eventual use in diabetes mellitus. As part of a programme investigating fluorescent glucose sensors, we have developed fibre-optic biosensors using glucose/galactose binding protein (GBP) labelled with the environmentally sensitive fluorophore, Badan. GBP-Badan was attached via an oligohistidine-tag to the surface of Ni-nitrilotriacetic acid (NTA)-functionalized agarose or polystyrene beads. Fluorescence lifetime increased in response to glucose, observed by fluorescence lifetime imaging microscopy of the GBP-Badan-beads. Either GBP-Badan agarose or polystyrene beads were loaded into a porous chamber at the end of a multimode optical fibre. Fluorescence lifetime responses were recorded using pulsed laser excitation, high speed photodiode detection and time-correlated singlephoton counting. The maximal response was at 100 mM glucose with an apparent K d of 13 mM (agarose) and 20 mM (polystyrene), and good working-day stability was demonstrated. We conclude that fluorescence lifetime fibre-optic glucose sensors based on GBP-Badan are suitable for development as clinical glucose monitors.

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Section: Ni-nta Agarose Beads For Binding Gbp-badancontrasting

confidence: 53%

Section: 20mentioning

confidence: 99%

A fluorescence lifetime-based fibre-optic glucose sensor using glucose/galactose-binding protein

Saxl

Khan

Ferla

et al. 2011

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“…The fluorescence lifetime of Badan-labeled glucose/galactose-binding protein (GBP) increases with increasing glucose concentration, which comes from the change to a more hydrophobic environment around Badan with the binding of GBP to glucose. 62 The fluorescence of Badan-labeled GBP exhibited a biexponential decay with a short-lifetime component of the free protein (~0.8 ns) and a long-lifetime component of the protein bound to glucose (~3.1 ns). 62 The fluorescence lifetimes of [1,3]dioxolo [4,5- 63 and ruthenium dipyridophenazine complexes 64 are also influenced by polar environments, which is applicable for the sensing of hydrophobic environments.…”

Section: ·7 Sensing Of Other Environementsmentioning

confidence: 98%

“…62 The fluorescence of Badan-labeled GBP exhibited a biexponential decay with a short-lifetime component of the free protein (~0.8 ns) and a long-lifetime component of the protein bound to glucose (~3.1 ns). 62 The fluorescence lifetimes of [1,3]dioxolo [4,5- 63 and ruthenium dipyridophenazine complexes 64 are also influenced by polar environments, which is applicable for the sensing of hydrophobic environments. The cyanine dye LS-288, which shows the near-infrared emission, exhibited an increase in the fluorescence lifetime with binding to protein, which has a high potential to monitor protein-losing nephropathy, due to diabetes mellitus.…”

Section: ·7 Sensing Of Other Environementsmentioning

confidence: 98%

Sensing of Intracellular Environments by Fluorescence Lifetime Imaging of Exogenous Fluorophores

Nakabayashi

Ohta

2015

ANAL. SCI.

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Fluorescence lifetime imaging (FLIM) has been recognized as a powerful microscopy technique to examine environments in living systems. The fluorescence lifetime does not depend on the photobleaching and optical conditions, which allows us to obtain quantitative information on intracellular environments by analyzing the fluorescence lifetime. A variety of exogenous fluorophores have been applied in FLIM measurements to examine cellular processes. Information on the correlation between the fluorescence lifetime and the physiological parameters is essential to elucidate the cellular environments from the fluorescence lifetime measurements of exogenous fluorophores. In this review, exogenous fluorophores used for lifetime-based sensing are summarized, with the expectation that it becomes a basis for selecting the fluorophore used to investigate the intracellular environment with FLIM. Experimental results of the intracellular sensing of pH, metal ions, oxygen, viscosity, and other physiological parameters on the basis of the FLIM measurements are described along with a brief explanation of the mechanism of the change in the fluorescence lifetime.

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“…A promising alternative to electrochemistry has been investigated by several research groups which is fluorescence-based glucose sensing [2,7,8]. This is a powerful method suitable for fast, sensitive, reagentless, and non-invasive detection of neutral analytes such as glucose [7][8][9].…”

Section: Introductionmentioning

confidence: 99%

Non-enzymatic assay for glucose by using immobilized whole-cells of E. coli containing glucose binding protein fused to fluorescent proteins

Charneca

Karmali

Vieira

2015

Sensors and Actuators B: Chemical

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Genetically encoded nanosensor 3.2 mM High throughput glucose assay Immobilization on 96-well microtiter plates FRET a b s t r a c t Glucose monitoring in vivo is a crucial issue for gaining new understanding of diabetes. Glucose binding protein (GBP) fused to two fluorescent indicator proteins (FLIP) was used in the present study such as FLIP-glu-3.2 mM. Recombinant Escherichia coli whole-cells containing genetically encoded nanosensors as well as cell-free extracts were immobilized either on inner epidermis of onion bulb scale or on 96-well microtiter plates in the presence of glutaraldehyde. Glucose monitoring was carried out by Förster Resonance Energy Transfer (FRET) analysis due the cyano and yellow fluorescent proteins (ECFP and EYFP) immobilized in both these supports.The recovery of these immobilized FLIP nanosensors compared with the free whole-cells and cell-free extract was in the range of 50-90%. Moreover, the data revealed that these FLIP nanosensors can be immobilized in such solid supports with retention of their biological activity. Glucose assay was devised by FRET analysis by using these nanosensors in real samples which detected glucose in the linear range of 0-24 mM with a limit of detection of 0.11 mM glucose. On the other hand, storage and operational stability studies revealed that they are very stable and can be re-used several times (i.e. at least 20 times) without any significant loss of FRET signal. To author's knowledge, this is the first report on the use of such immobilization supports for whole-cells and cell-free extract containing FLIP nanosensor for glucose assay. On the other hand, this is a novel and cheap high throughput method for glucose assay.

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Fluorescence lifetime spectroscopy and imaging of nano-engineered glucose sensor microcapsules based on glucose/galactose-binding protein

Cited by 60 publications

References 37 publications

A fluorescence lifetime-based fibre-optic glucose sensor using glucose/galactose-binding protein

A fluorescence lifetime-based fibre-optic glucose sensor using glucose/galactose-binding protein

Sensing of Intracellular Environments by Fluorescence Lifetime Imaging of Exogenous Fluorophores

Non-enzymatic assay for glucose by using immobilized whole-cells of E. coli containing glucose binding protein fused to fluorescent proteins

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