Integrated Visible optical filter and photodetector for detection of FRET signals

2014 ◽  
Vol 1689 ◽  
Author(s):  
P. Louro ◽  
A. Charneca ◽  
V. Silva ◽  
M. Vieira ◽  
A. Karmali
Keyword(s):  
Optical Filter ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Protein Detection ◽  
Free Form ◽  
Visible Range ◽  
Wavelength Band ◽  
Selective Sensitivity ◽  
Device Sensitivity ◽  
Electrical Bias

ABSTRACTIn this paper we present a multilayer device based on a-Si:H/a-SiC:H that operates as photodetector and optical filter. The use of such device in protein detection applications is pertinent in Fluorescence Resonance Energy Transfer (FRET) measurements that demand the detection of visible fluorescent signals located at specific wavelengths bands. This device was designed to operate in the visible range with a selective sensitivity dependent on the applied electrical bias. Several nanosensors were tested with a commercial spectrophotometer to judge the performance of the FRET signals using glucose solutions of different concentrations. Two nanosensors (FLIPglu-90μM and FLIPglu-600μM) were tested with a commercial spectrofluorimeter to judge the performance of the FRET signals by using glucose solutions of different concentrations. These measurements were carried out by using these nanosensors both in the free form and immobilized form on inner epidermis of onion bulb scale. The proposed device was used to demonstrate the possibility of FRET signals detection, using visible signals of similar wavelength and intensity. The device sensitivity was tuned to enhance the wavelength band of interest using adequate electrical biasing.

scholarly journals Synthesis of NaYF4:Yb/Er/Gd up-conversion luminescent nanoparticles and luminescence resonance energy transfer-based protein detection

2012 ◽  
Vol 421 (2) ◽  
pp. 673-679 ◽  
Author(s):  
Jingpu Zhang ◽  
Congcong Mi ◽  
Hongyan Wu ◽  
Huaiqing Huang ◽  
Chuanbin Mao ◽  
...  
Keyword(s):  
Energy Transfer ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Protein Detection ◽  
Luminescent Nanoparticles

Aptamer-based rolling circle amplification coupled with graphene oxide-based fluorescence resonance energy transfer for sensitive detection of cardiac troponin I

2018 ◽  
Vol 10 (15) ◽  
pp. 1767-1773 ◽  
Author(s):  
Yu Li ◽  
Weiqiang Dai ◽  
Xuefei Lv ◽  
Yulin Deng
Keyword(s):  
Graphene Oxide ◽  
Energy Transfer ◽  
Fluorescence Resonance Energy Transfer ◽  
Troponin I ◽  
Rolling Circle Amplification ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Protein Detection ◽  
Rolling Circle ◽  
Fluorescence Resonance

Combining the high affinity and specificity of an aptamer for a protein, a highly sensitive strategy for protein detection was developed based on rolling circle amplification (RCA) and graphene oxide based fluorescence resonance energy transfer (FRET).

scholarly journals Development of FRET-Based Assays in the Far-Red Using CdTe Quantum Dots

2007 ◽  
Vol 2007 ◽  
pp. 1-7 ◽  
Author(s):  
E. Z. Chong ◽  
D. R Matthews ◽  
H. D. Summers ◽  
K. L. Njoh ◽  
R. J. Errington ◽  
...  
Keyword(s):  
Quantum Dots ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Fluorescence Decay ◽  
Cdte Quantum Dots ◽  
Visible Range ◽  
Biological Perspective ◽  
Biotin Binding ◽  
Donor Acceptor ◽  
Long Lifetime

Colloidal quantum dots (QDs) are now commercially available in a biofunctionalized form, and Förster resonance energy transfer (FRET) between bioconjugated dots and fluorophores within the visible range has been observed. We are particularly interested in the far-red region, as from a biological perspective there are benefits in pushing to∼700 nm to minimize optical absorption (ABS) within tissue and to avoid cell autofluorescence. We report on FRET between streptavidin- (STV-) conjugated CdTe quantum dots, Qdot705-STV, with biotinylated DY731-Bio fluorophores in a donor-acceptor assay. We also highlight the changes in DY731-Bio absorptivity during the streptavidin-biotin binding process which can be attributed to the structural reorientation. For fluorescence beyond 700 nm, different alloy compositions are required for the QD core and these changes directly affect the fluorescence decay dynamics producing a marked biexponential decay with a long-lifetime component in excess of 100 nanoseconds. We compare the influence of the two QD relaxation routes upon FRET dynamics in the presence of DY731-Bio.

scholarly journals Spectral-Time Multiplexing in FRET Complexes of AgInS2/ZnS Quantum Dot and Organic Dyes

Nanomaterials ◽  
2020 ◽  
Vol 10 (8) ◽  
pp. 1569 ◽  
Author(s):  
Vera Kuznetsova ◽  
Anton Tkach ◽  
Sergei Cherevkov ◽  
Anastasiia Sokolova ◽  
Yulia Gromova ◽  
...  
Keyword(s):  
Quantum Dots ◽  
Organic Dyes ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Visible Range ◽  
Additional Parameter ◽  
Time Resolved ◽  
Cd Toxicity ◽  
Multiplex Analysis ◽  
Luminescent Markers

Nowadays, multiplex analysis is very popular, since it allows to detect a large number of biomarkers simultaneously. Traditional multiplex analysis is usually based on changes of photoluminescence (PL) intensity and/or PL band spectral positions in the presence of analytes. Using PL lifetime as an additional parameter might increase the efficiency of multiplex methods. Quantum dots (QDs) can be used as luminescent markers for multiplex analysis. Ternary in-based QDs are a great alternative to the traditional Cd-based one. Ternary QDs possess all advantages of traditional QDs, including tunable photoluminescence in visible range. At the same time ternary QDs do not have Cd-toxicity, and moreover they possess long spectral dependent lifetimes. This allows the use of ternary QDs as a donor for time-resolved multiplex sensing based on Förster resonance energy transfer (FRET). In the present work, we implemented FRET from AgInS2/ZnS ternary QDs to cyanine dyes absorbing in different spectral regions of QD luminescence with different lifetimes. As the result, FRET-induced luminescence of dyes differed not only in wavelengths but also in lifetimes of luminescence, which can be used for time-resolved multiplex analysis in biology and medicine.

Characterization of a monolithic device for detection of FRET signals

2012 ◽  
Vol 1426 ◽  
pp. 187-192 ◽  
Author(s):  
P. Louro ◽  
M. Vieira ◽  
M. A. Vieira ◽  
V. Silva ◽  
J. Costa
Keyword(s):  
Fluorescent Proteins ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Standard Technique ◽  
Cost Effective ◽  
Optical Filters ◽  
Visible Range ◽  
Optical Signals ◽  
Mechanical Parts

ABSTRACTFluorescence Resonance Energy Transfer (FRET) is a standard technique used in many medical and biological applications. It involves the detection of transient fluorescent signals coming from the different fluorescent proteins that work in the visible range of the spectrum. Common fluorescent emissions come from the cyan/yellow fluorophores that emit respectively, at 470 nm and 588 nm. In this paper we use optical filters based on multilayered a-SiC:H heterostructures to detect optical signals at these wavelengths. The advantage of this type of sensor is that it does not rely on mechanical parts; it is compact and cost effective. The transducer consists of two heterostructures based on a-SiC:H/a-Si:H optimized for the detection of the fluorescence emissions at wavelengths 470 nm (cyan) and 588 nm (yellow). Both front and back structures were designed to optimize the detection at these wavelengths. Results show that the device photocurrent signal measured under reverse bias and using appropriate steady state optical bias, allows the separate detection of the cyan and yellow fluorescence signals.

Structural dynamics of P-type ATPase ion pumps

2019 ◽  
Vol 47 (5) ◽  
pp. 1247-1257 ◽  
Author(s):  
Mateusz Dyla ◽  
Sara Basse Hansen ◽  
Poul Nissen ◽  
Magnus Kjaergaard
Keyword(s):  
Structural Dynamics ◽  
Single Molecule ◽  
New Technologies ◽  
Atp Hydrolysis ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Time Resolved ◽  
Dynamics Simulations ◽  
Types Of Information ◽  
P Type

Abstract P-type ATPases transport ions across biological membranes against concentration gradients and are essential for all cells. They use the energy from ATP hydrolysis to propel large intramolecular movements, which drive vectorial transport of ions. Tight coordination of the motions of the pump is required to couple the two spatially distant processes of ion binding and ATP hydrolysis. Here, we review our current understanding of the structural dynamics of P-type ATPases, focusing primarily on Ca2+ pumps. We integrate different types of information that report on structural dynamics, primarily time-resolved fluorescence experiments including single-molecule Förster resonance energy transfer and molecular dynamics simulations, and interpret them in the framework provided by the numerous crystal structures of sarco/endoplasmic reticulum Ca2+-ATPase. We discuss the challenges in characterizing the dynamics of membrane pumps, and the likely impact of new technologies on the field.

Quantum Dot Bioconjugates as Energy Donors in Fluorescence Resonance Energy Transfer Assays

2003 ◽  
Vol 773 ◽  
Author(s):  
Aaron R. Clapp ◽  
Igor L. Medintz ◽  
J. Matthew Mauro ◽  
Hedi Mattoussi
Keyword(s):  
Energy Transfer ◽  
Quantum Dot ◽  
Organic Dyes ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Genetically Engineered ◽  
Molar Ratio ◽  
Binding Assays ◽  
Specific Sequence ◽  
Donor Acceptor

AbstractLuminescent CdSe-ZnS core-shell quantum dot (QD) bioconjugates were used as energy donors in fluorescent resonance energy transfer (FRET) binding assays. The QDs were coated with saturating amounts of genetically engineered maltose binding protein (MBP) using a noncovalent immobilization process, and Cy3 organic dyes covalently attached at a specific sequence to MBP were used as energy acceptor molecules. Energy transfer efficiency was measured as a function of the MBP-Cy3/QD molar ratio for two different donor fluorescence emissions (different QD core sizes). Apparent donor-acceptor distances were determined from these FRET studies, and the measured distances are consistent with QD-protein conjugate dimensions previously determined from structural studies.

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