Multicolor In Vivo Imaging of Upconversion Nanoparticles with Emissions Tuned by Luminescence Resonance Energy Transfer

2011 ◽  
Vol 115 (6) ◽  
pp. 2686-2692 ◽  
Author(s):  
Liang Cheng ◽  
Kai Yang ◽  
Mingwang Shao ◽  
Shuit-Tong Lee ◽  
Zhuang Liu
Keyword(s):  
Energy Transfer ◽  
In Vivo Imaging ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Upconversion Nanoparticles

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 Nanoscale optical writing through upconversion resonance energy transfer

2021 ◽  
Vol 7 (9) ◽  
pp. eabe2209
Author(s):  
S. Lamon ◽  
Y. Wu ◽  
Q. Zhang ◽  
X. Liu ◽  
M. Gu
Keyword(s):  
Graphene Oxide ◽  
Energy Transfer ◽  
Energy Consumption ◽  
Data Storage ◽  
High Capacity ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
High Energy ◽  
Optical Data ◽  
Upconversion Nanoparticles

Nanoscale optical writing using far-field super-resolution methods provides an unprecedented approach for high-capacity data storage. However, current nanoscale optical writing methods typically rely on photoinitiation and photoinhibition with high beam intensity, high energy consumption, and short device life span. We demonstrate a simple and broadly applicable method based on resonance energy transfer from lanthanide-doped upconversion nanoparticles to graphene oxide for nanoscale optical writing. The transfer of high-energy quanta from upconversion nanoparticles induces a localized chemical reduction in graphene oxide flakes for optical writing, with a lateral feature size of ~50 nm (1/20th of the wavelength) under an inhibition intensity of 11.25 MW cm−2. Upconversion resonance energy transfer may enable next-generation optical data storage with high capacity and low energy consumption, while offering a powerful tool for energy-efficient nanofabrication of flexible electronic devices.

scholarly journals Contribution of resonance energy transfer to the luminescence quenching of upconversion nanoparticles with graphene oxide

2020 ◽  
Vol 575 ◽  
pp. 119-129 ◽  
Author(s):  
Diego Mendez-Gonzalez ◽  
Oscar G. Calderón ◽  
Sonia Melle ◽  
Jesús González-Izquierdo ◽  
Luis Bañares ◽  
...  
Keyword(s):  
Graphene Oxide ◽  
Energy Transfer ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Luminescence Quenching ◽  
Upconversion Nanoparticles

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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