Fluorescence Glucose Detection: Advances Toward the Ideal In Vivo Biosensor

Moschou, Elizabeth A.; Sharma, Bethel V.; Deo, Sapna K.; Daunert, Sylvia

doi:10.1023/b:jofl.0000039341.64999.83

Cited by 142 publications

(76 citation statements)

References 26 publications

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“…It has been proposed that users could assess their glucose concentration by comparing the colour of their contact lens against pre-calibrated colour strip (Badugu et al, 2005). Further work is needed to address issues of resolution, lifetime and biocompatibility (Moschou et al, 2004). The main issues concerning this method are, firstly, it seems that glucose fluctuation would only be detected if its concentration increased over what was expected.…”

Section: Less Invasive Approaches To Health Monitoringmentioning

confidence: 99%

Minimally Invasive Sensing

McCormick¹,

Heath²,

Connolly³

2011

Biosensors - Emerging Materials and Applications

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Section: Less Invasive Approaches To Health Monitoringmentioning

confidence: 99%

Minimally Invasive Sensing

McCormick¹,

Heath²,

Connolly³

2011

Biosensors - Emerging Materials and Applications

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“…Numerous efforts have been made to develop systems that detect glucose in vivo (26). The most common sensors are glucose-oxidase-based; in addition, several groups have worked toward using naturally occurring periplasmic GBP.…”

Section: Biomedical Sensingmentioning

confidence: 99%

Hinge-Motion Binding Proteins: Unraveling Their Analytical Potential

Moschou¹,

Bachas²,

Daunert³

et al. 2006

Anal. Chem.

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C hemical analysis has benefited significantly from recent advances in instrumentation that enhance detection sensitivity. The complexity of sample matrices and the presence of compounds structurally related to an analyte dictate the need for sensitive and selective methods that can discriminate the analyte from interferences. Research has focused on the discovery of synthetic molecular recognition systems, referred to as host-guest chemistry, as well as the identification of biological recognition systems. Among such biomolecules, hinge-motion binding proteins (HMBPs) demonstrate exquisite selectivity toward their corresponding ligand/analyte, with affinities K D down to the nanomolar range. These proteins are so named because they undergo a significant conformational change upon binding of the ligand-the two domains bend around a "hinge" region of the protein. The binding mechanism of these proteins resembles that of the carnivorous plant commonly known as the Venus flytrap.The conformational change that HMBPs undergo upon binding of a ligand can be used to quantify a target analyte. In one approach, a reporter group, such as a fluorescent probe, is strategically positioned on the protein so that it experiences a change in its microenvironment as a result of a binding event (Figure 1a). Another method involves protein chimeras, in which the HMBP is fused with other proteins and the signal is transduced upon binding with the target analyte (Figure 1b). In a third technique, the HMBP can be labeled with a reporter molecule, which moves as a result of the binding event either closer to or further away from the signal transducer (Figure 1c). A fourth strategy uses the conformational change to enable the expression of a reporter molecule through a transcriptional regulation mechanism (Figure 1d).Different classes of HMBPs include periplasmic binding proteins; transcriptional regulators; enzymes; and messenger proteins, like calmodulin (1). This article focuses on periplasmic binding proteins and calmodulin, because they have already been applied to environmental and metabolite monitoring, food technology, bioanalysis, high-throughput screening, and diagnostics.Hinge-motion binding proteins undergo a conformational change that can be used as the basis for quantifying analytes.

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“…Although many glucose sensing systems have found in vivo applications, the need for a reliable, specific, sensitive and stable glucose sensor is highly required [4]. There are many parameters that affect the development of an optimized glucose sensor such as selectivity, linear range, biocompatibility, response time, reproducibility and reversibility of signal [5]. Moreover, these enzyme electrodes are based on a chemical conversion [6] with a consumption of glucose and O 2 and production of hydrogen peroxide and d-gluconic acid in vivo.…”

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 Glucose Detection: Advances Toward the Ideal In Vivo Biosensor

Cited by 142 publications

References 26 publications

Minimally Invasive Sensing

Minimally Invasive Sensing

Hinge-Motion Binding Proteins: Unraveling Their Analytical Potential

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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