scholarly journals Near-Infrared Resonance Energy Transfer Glucose Biosensors in Hybrid Microcapsule Carriers

2008 ◽  
Vol 2008 ◽  
pp. 1-11 ◽  
Author(s):  
Swetha Chinnayelka ◽  
Huiguang Zhu ◽  
Mike McShane
Keyword(s):  
Energy Transfer ◽  
Continuous Monitoring ◽  
Near Infrared ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Competitive Binding ◽  
Competitive Binding Assay ◽  
Sensing Systems ◽  
Recent Developments

Fluorescence-based sensing systems offer potential for noninvasive monitoring with implantable devices, but require carrier technologies that provide suitable immobilization, accessibility, and biocompatibility. Recent developments towards this goal include a competitive binding assay for glucose that has been encapsulated in semipermeable microcapsule carriers. This paper describes an extension of this work to increase the applicability to in vivo monitoring, wherein two significant developments are described: (1) a near-infrared resonance energy transfer system for transducing glucose concentration, and (2) novel hybrid organic-inorganic crosslinked microcapsules as carriers. The quenching-based assay is a competitive binding (CB) system based on apo-glucose oxidase (AG) as the receptor and dextran as the competitive ligand. The encapsulated quencher-labeled dextran and near infrared donor-labeled glucose receptor showed a stable and reversible response with tunable sensitivity of 1–5%/mM over the physiological range, making these transducers attractive for continuous monitoring for biomedical applications.

Nanoparticles based on quantum dots and a luminol derivative: implications for in vivo imaging of hydrogen peroxide by chemiluminescence resonance energy transfer

2016 ◽  
Vol 52 (22) ◽  
pp. 4132-4135 ◽  
Author(s):  
Eun Sook Lee ◽  
V. G. Deepagan ◽  
Dong Gil You ◽  
Jueun Jeon ◽  
Gi-Ra Yi ◽  
...  
Keyword(s):  
Hydrogen Peroxide ◽  
Energy Transfer ◽  
In Vivo Imaging ◽  
Near Infrared ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Hybrid Nanoparticles ◽  
Infrared Wavelength ◽  
Luminol Derivative

Hybrid nanoparticles allow for imaging hydrogen peroxide via chemiluminescence resonance energy transfer in the near-infrared wavelength range.

scholarly journals Measuring ligand-dependent and ligand-independent interactions between nuclear receptors and associated proteins using Bioluminescence Resonance Energy Transfer (BRET2)

2006 ◽  
Vol 4 (1) ◽  
pp. nrs.04021 ◽  
Author(s):  
Kristen L. Koterba ◽  
Brian G. Rowan
Keyword(s):  
Energy Transfer ◽  
Protein Interactions ◽  
Fusion Proteins ◽  
Fluorescent Protein ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Renilla Luciferase ◽  
Receptor Protein ◽  
Protein Protein Interactions

Bioluminescent resonance energy transfer (BRET2) is a recently developed technology for the measurement of protein-protein interactions in a live, cell-based system. BRET2 is characterized by the efficient transfer of excited energy between a bioluminescent donor molecule (Renilla luciferase) and a fluorescent acceptor molecule (a mutant of Green Fluorescent Protein (GFP2)). The BRET2 assay offers advantages over fluorescence resonance energy transfer (FRET) because it does not require an external light source thereby eliminating problems of photobleaching and autoflourescence. The absence of contamination by light results in low background that permits detection of very small changes in the BRET2 signal. BRET2 is dependent on the orientation and distance between two fusion proteins and therefore requires extensive preliminary standardization experiments to conclude a positive BRET2 signal independent of variations in protein titrations and arrangement in tertiary structures. Estrogen receptor (ER) signaling is modulated by steroid receptor coactivator 1 (SRC-1). To establish BRET2 in a ligand inducible system we used SRC-1 as the donor moiety and ER as the acceptor moiety. Expression and functionality of the fusion proteins were assessed by transient transfection in HEK-293 cells followed by Western blot analysis and measurement of ER-dependent reporter gene activity. These preliminary determinations are required prior to measuring nuclear receptor protein-protein interactions by BRET2. This article describes in detail the BRET2 methodology for measuring interaction between full-length ER and coregulator proteins in real-time, in an in vivo environment.

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