Dual Förster resonance energy transfer effects in non-fullerene ternary organic solar cells with the third component embedded in the donor and acceptor

2017 ◽  
Vol 5 (24) ◽  
pp. 12120-12130 ◽  
Author(s):  
Pengqing Bi ◽  
Fei Zheng ◽  
Xiaoyu Yang ◽  
Mengsi Niu ◽  
Lin Feng ◽  
...  
Keyword(s):  
Energy Transfer ◽  
Ternary System ◽  
Organic Solar Cells ◽  
Phase Distribution ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Transfer Effects ◽  
The Third ◽  
System P ◽  
Donor And Acceptor

An investigation of phase distribution demonstrated that PCDTBT was embedded in PTB7-Th and ITIC, and hence introduced dual FRET effects in the resulting ternary system.

Enhanced light harvesting through Förster resonance energy transfer in polymer–small molecule ternary system

2017 ◽  
Vol 5 (5) ◽  
pp. 1136-1148 ◽  
Author(s):  
Amreen A. Hussain ◽  
Arup R. Pal
Keyword(s):  
Energy Transfer ◽  
Ternary System ◽  
Performance Enhancement ◽  
Light Harvesting ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Ternary Blend ◽  
New Approach ◽  
System P ◽  
Ternary Structure

A conceptually new approach to fabricate a robust ternary structure is introduced for light harvesting devices. An interesting photophysical mechanism of the ternary blend in a real device is highlighted where FRET strongly contributes to the performance enhancement of the device.

scholarly journals Dual Förster resonance energy transfer and morphology control to boost the power conversion efficiency of all-polymer OPVs

RSC Advances ◽  
2017 ◽  
Vol 7 (22) ◽  
pp. 13289-13298 ◽  
Author(s):  
Jiangang Liu ◽  
Bin Tang ◽  
Qiuju Liang ◽  
Yanchun Han ◽  
Zhiyuan Xie ◽  
...  
Keyword(s):  
Energy Transfer ◽  
Power Conversion ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Forster Resonance Energy Transfer ◽  
Förster Resonance Energy Transfer ◽  
Ternary Blend ◽  
The Third ◽  
System P ◽  
Förster Resonance

Dual Förster resonance energy transfer was developed in a PTB7-Th (donor)/P(NDI2OD-T2) (accepter)/PF12TBT (the third component) ternary blend system.

scholarly journals Distribution of a Glycosylphosphatidylinositol-anchored Protein at the Apical Surface of MDCK Cells Examined at a Resolution of <100 Å Using Imaging Fluorescence Resonance Energy Transfer

1998 ◽  
Vol 142 (1) ◽  
pp. 69-84 ◽  
Author(s):  
A.K. Kenworthy ◽  
M. Edidin
Keyword(s):  
Energy Transfer ◽  
Lipid Rafts ◽  
Fluorescence Resonance Energy Transfer ◽  
Mdck Cells ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Membrane Microdomains ◽  
Apical Surface ◽  
Donor And Acceptor ◽  
Fluorescence Resonance

Membrane microdomains (“lipid rafts”) enriched in glycosylphosphatidylinositol (GPI)-anchored proteins, glycosphingolipids, and cholesterol have been implicated in events ranging from membrane trafficking to signal transduction. Although there is biochemical evidence for such membrane microdomains, they have not been visualized by light or electron microscopy. To probe for microdomains enriched in GPI- anchored proteins in intact cell membranes, we used a novel form of digital microscopy, imaging fluorescence resonance energy transfer (FRET), which extends the resolution of fluorescence microscopy to the molecular level (&lt;100 Å). We detected significant energy transfer between donor- and acceptor-labeled antibodies against the GPI-anchored protein 5′ nucleotidase (5′ NT) at the apical membrane of MDCK cells. The efficiency of energy transfer correlated strongly with the surface density of the acceptor-labeled antibody. The FRET data conformed to theoretical predictions for two-dimensional FRET between randomly distributed molecules and were inconsistent with a model in which 5′ NT is constitutively clustered. Though we cannot completely exclude the possibility that some 5′ NT is in clusters, the data imply that most 5′ NT molecules are randomly distributed across the apical surface of MDCK cells. These findings constrain current models for lipid rafts and the membrane organization of GPI-anchored proteins.

Energy transfer in ternary blend organic solar cells: recent insights and future directions

2021 ◽  
Author(s):  
Aiswarya Abhisek Mohapatra ◽  
Vivek Tiwari ◽  
Satish Patil
Keyword(s):  
Energy Transfer ◽  
Solar Cells ◽  
Organic Solar Cells ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Ternary Blend ◽  
Future Directions ◽  
Photosynthetic Proteins

Resonance energy transfer in ternary blend organic solar cells is discussed by drawing parallels from natural photosynthetic proteins.

Effect of compartmentalization of donor and acceptor on the ultrafast resonance energy transfer from DAPI to silver nanoclusters

Nanoscale ◽  
2016 ◽  
Vol 8 (26) ◽  
pp. 13006-13016 ◽  
Author(s):  
Roopali Prajapati ◽  
Surajit Chatterjee ◽  
Krishna K. Kannaujiya ◽  
Tushar Kanti Mukherjee
Keyword(s):  
Energy Transfer ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Silver Nanoclusters ◽  
Donor And Acceptor

scholarly journals Versatility of Homogeneous Time-Resolved Fluorescence Resonance Energy Transfer Assays for Biologics Drug Discovery

2014 ◽  
Vol 20 (4) ◽  
pp. 508-518 ◽  
Author(s):  
Christine J. Rossant ◽  
Carl Matthews ◽  
Frances Neal ◽  
Caroline Colley ◽  
Matthew J. Gardener ◽  
...  
Keyword(s):  
Energy Transfer ◽  
Drug Discovery ◽  
Fluorescence Resonance Energy Transfer ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Time Resolved Fluorescence ◽  
Time Resolved ◽  
Donor And Acceptor ◽  
Wide Range ◽  
Fluorescence Resonance

Identification of potential lead antibodies in the drug discovery process requires the use of assays that not only measure binding of the antibody to the target molecule but assess a wide range of other characteristics. These include affinity ranking, measurement of their ability to inhibit relevant protein-protein interactions, assessment of their selectivity for the target protein, and determination of their species cross-reactivity profiles to support in vivo studies. Time-resolved fluorescence resonance energy transfer is a technology that offers the flexibility for development of such assays, through the availability of donor and acceptor fluorophore-conjugated reagents for detection of multiple tags or fusion proteins. The time-resolved component of the technology reduces potential assay interference, allowing screening of a range of different crude sample types derived from the bacterial or mammalian cell expression systems often used for antibody discovery projects. Here we describe the successful application of this technology across multiple projects targeting soluble proteins and demonstrate how it has provided key information for the isolation of potential therapeutic antibodies with the desired activity profile.

Measurement of proteases using chemiluminescence-resonance-energy-transfer chimaeras between green fluorescent protein and aequorin

2001 ◽  
Vol 357 (3) ◽  
pp. 687-697 ◽  
Author(s):  
Jonathan P. WAUD ◽  
Alexandra BERMÚDEZ FAJARDO ◽  
Thankiah SUDHAHARAN ◽  
Andrew R. TRIMBY ◽  
Jinny JEFFERY ◽  
...  
Keyword(s):  
Energy Transfer ◽  
Green Fluorescent Protein ◽  
Caspase 3 ◽  
Fluorescent Protein ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Dependent Manner ◽  
Cell Extracts ◽  
Donor And Acceptor ◽  
Green Fluorescent

Homogeneous assays, without a separation step, are essential for measuring chemical events in live cells and for drug discovery screens, and are desirable for making measurements in cell extracts or clinical samples. Here we demonstrate the principle of chemiluminescence resonance energy transfer (CRET) as a homogeneous assay system, using two proteases as models, one extracellular (α-thrombin) and the other intracellular (caspase-3). Chimaeras were engineered with aequorin as the chemiluminescent energy donor and green fluorescent protein (GFP) or enhanced GFP as the energy acceptors, with a protease linker (6 or 18 amino acid residues) recognition site between the donor and acceptor. Flash chemiluminescent spectra (20–60 s) showed that the spectra of chimaeras matched GFP, being similar to that of luminous jellyfish, justifying their designation as ‘Rainbow’ proteins. Addition of the protease shifted the emission spectrum to that of aequorin in a time- and dose-dependent manner. Separation of the proteolysed fragments showed that the ratio of green to blue light matched the extent of proteolysis. The caspase-3 Rainbow protein was able to provide information on the specificity of caspases in vitro and in vivo. It was also able to monitor caspase-3 activation in cells provoked into apoptosis by staurosporine (1 or 2μM). CRET can also monitor GFP fluor formation. The signal-to-noise ratio of our Rainbow proteins is superior to that of fluorescence resonance energy transfer, providing a potential platform for measuring agents that interact with the reactive site between the donor and acceptor.

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