Special Issue "FRET-Based Biosensors"

A special issue of Biosensors (ISSN 2079-6374).

Deadline for manuscript submissions: closed (1 December 2018)

Special Issue Editor

Guest Editor
Dr. Karl David Wegner

INAC Institute for Nanoscience and Cryogenics; French Alternative Energies and Atomic Energy Commission, CEA-Grenoble, France
Website | E-Mail
Interests: biosensors; FRET; immunoassays; multiplexing; quantum dots; spectroscopy; imaging; nanoparticle synthesis

Special Issue Information

Dear Colleagues,

In the last few decades, Förster resonance energy transfer (FRET) has become an established method for the sensitive detection of various targets in numerous biosensing applications. FRET is a non-radiative energy transfer from an excited donor to an acceptor at a close distance (a few nanometres). The high distance sensitivity makes it a preferred tool for qualitative and quantitative analyses of biological interactions and processes. The utilization of new fluorescent materials, such as semiconductor nanocrystals, upconversion nanoparticles, fluorescent polymers, metal chelates, various noble metal and other nanoparticles, have greatly fostered advancements in the design of biosensors. FRET biosensors combining these robust fluorophores with new sensor designs enabled translation from the utilization of sophisticated benchtop fluorescent spectrometers to simple point-of-care devices for the assessment of biomarkers, drugs, environmental pollution, and for food quality analysis.

In this Special Issue, manuscripts are invited, which are devoted to the application of FRET for designing various types of sensors. Both reviews and original research articles will be published. Reviews should provide a critical overview of the current state-of-the-art in a particular application field, such as in vitro diagnostics, food safety and quality control or environmental pollution. Critical overviews about the use of a specific fluorophores, such as semiconductor nanocrystals or other nanoparticles in FRET-based biosensing applications, are also of interest. Original research papers that present new FRET-based sensor designs and/or fundamental studies with potential relevance to biosensing are also welcome.

Dr. Karl David Wegner
Guest Editor

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All papers will be peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Biosensors is an international peer-reviewed open access quarterly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 650 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • FRET
  • luminescence
  • nanotechnology
  • nanomaterials
  • fluorescent probes
  • diagnostics
  • bioanalysis
  • point-of-care
  • imaging
  • food safety
  • environmental pollution

Published Papers (5 papers)

View options order results:
result details:
Displaying articles 1-5
Export citation of selected articles as:

Research

Jump to: Review

Open AccessArticle
In-Vitro Characterization of mCerulean3_mRuby3 as a Novel FRET Pair with Favorable Bleed-Through Characteristics
Biosensors 2019, 9(1), 33; https://doi.org/10.3390/bios9010033
Received: 1 December 2018 / Revised: 12 February 2019 / Accepted: 19 February 2019 / Published: 28 February 2019
PDF Full-text (3444 KB) | HTML Full-text | XML Full-text | Supplementary Files
Abstract
In previous studies, we encountered substantial problems using the CFP_YFP Förster resonance energy transfer (FRET) pair to analyze protein proximity in the endoplasmic reticulum of live cells. Bleed-through of the donor emission into the FRET channel and overlap of the FRET emission wavelength [...] Read more.
In previous studies, we encountered substantial problems using the CFP_YFP Förster resonance energy transfer (FRET) pair to analyze protein proximity in the endoplasmic reticulum of live cells. Bleed-through of the donor emission into the FRET channel and overlap of the FRET emission wavelength with highly variable cellular autofluorescence significantly compromised the sensitivity of our analyses. Here, we propose mCerulean3 and mRuby3 as a new FRET pair to potentially overcome these problems. Fusion of the two partners with a trypsin-cleavable linker allowed the direct comparison of the FRET signal characteristics of the associated partners with those of the completely dissociated partners. We compared our new FRET pair with the canonical CFP_YFP and the more recent mClover3_mRuby3 pairs and found that, despite a lower total FRET signal intensity, the novel pair had a significantly better signal to noise ratio due to lower donor emission bleed-through. This and the fact that the mRuby3 emission spectrum did not overlap with that of common cellular autofluorescence renders the mCerulean3_mRuby3 FRET pair a promising alternative to the common CFP_YFP FRET pair for the interaction analysis of membrane proteins in living cells. Full article
(This article belongs to the Special Issue FRET-Based Biosensors)
Figures

Graphical abstract

Open AccessArticle
Energy Transfer between Tm-Doped Upconverting Nanoparticles and a Small Organic Dye with Large Stokes Shift
Biosensors 2019, 9(1), 9; https://doi.org/10.3390/bios9010009
Received: 29 November 2018 / Revised: 20 December 2018 / Accepted: 28 December 2018 / Published: 8 January 2019
Cited by 3 | PDF Full-text (5252 KB) | HTML Full-text | XML Full-text
Abstract
Lanthanide-doped upconverting nanoparticles (UCNP) are being extensively studied for bioapplications due to their unique photoluminescence properties and low toxicity. Interest in RET applications involving UCNP is also increasing, but due to factors such as large sizes, ion emission distributions within the particles, and [...] Read more.
Lanthanide-doped upconverting nanoparticles (UCNP) are being extensively studied for bioapplications due to their unique photoluminescence properties and low toxicity. Interest in RET applications involving UCNP is also increasing, but due to factors such as large sizes, ion emission distributions within the particles, and complicated energy transfer processes within the UCNP, there are still many questions to be answered. In this study, four types of core and core-shell NaYF4-based UCNP co-doped with Yb3+ and Tm3+ as sensitizer and activator, respectively, were investigated as donors for the Methyl 5-(8-decanoylbenzo[1,2-d:4,5-d′]bis([1,3]dioxole)-4-yl)-5-oxopentanoate (DBD-6) dye. The possibility of resonance energy transfer (RET) between UCNP and the DBD-6 attached to their surface was demonstrated based on the comparison of luminescence intensities, band ratios, and decay kinetics. The architecture of UCNP influenced both the luminescence properties and the energy transfer to the dye: UCNP with an inert shell were the brightest, but their RET efficiency was the lowest (17%). Nanoparticles with Tm3+ only in the shell have revealed the highest RET efficiencies (up to 51%) despite the compromised luminescence due to surface quenching. Full article
(This article belongs to the Special Issue FRET-Based Biosensors)
Figures

Figure 1

Open AccessArticle
Development of DNA Pair Biosensor for Quantization of Nuclear Factor Kappa B
Biosensors 2018, 8(4), 126; https://doi.org/10.3390/bios8040126
Received: 9 November 2018 / Revised: 29 November 2018 / Accepted: 5 December 2018 / Published: 10 December 2018
PDF Full-text (1081 KB) | HTML Full-text | XML Full-text
Abstract
Nuclear factor kappa B (NF-κB), regulating the expression of several genes that mediate the inflammatory responses and cell proliferation, is one of the therapeutic targets for chronic inflammatory disease and cancer. A novel molecular binding scheme for the detection of NF-κB was investigated [...] Read more.
Nuclear factor kappa B (NF-κB), regulating the expression of several genes that mediate the inflammatory responses and cell proliferation, is one of the therapeutic targets for chronic inflammatory disease and cancer. A novel molecular binding scheme for the detection of NF-κB was investigated for its affinity to Ig-κB DNA composed by dye and quencher fluorophores, and this specificity is confirmed by competing with the DNA sequence that is complementary to the Ig-κB DNA. We create a normalization equation to remove the negative effects from the various initial fluorophore concentrations and the background noise. We also found that a periodic shaking at a frequency could help to stabilize the DNA–protein binding. The calibration experiment, using purified p50 (NF-κB), shows that this molecular probe biosensor has a detection limit on the order of nanomolar. The limit of detection is determined by the binding performance of dye and quencher oligonucleotides, and only a small portion of probes are stabilized by DNA-binding protein NF-κB. The specificity experiment also shows that p50/p65 heterodimer has the highest affinity for Ig-κB DNA; p65 homodimer binds with intermediate affinity, whereas p50 shows the lowest binding affinity, and Ig-κB DNA is not sensitive to BSA (bovine albumin serum). The experiment of HeLa nuclear extract shows that TNF-α stimulated HeLa nuclear extract has higher affinity to Ig-κB DNA than non-TNF-stimulated HeLa nuclear extract (4-h serum response). Therefore, the molecular binding scheme provides a rapid, quantitative, high throughput, and automated measurement of the DNA-binding protein NF-κB at low cost, which is beneficial for automated drug screening systems. Full article
(This article belongs to the Special Issue FRET-Based Biosensors)
Figures

Figure 1

Open AccessArticle
A DNA-Based Assay for Digoxin Detection
Biosensors 2018, 8(1), 19; https://doi.org/10.3390/bios8010019
Received: 6 February 2018 / Revised: 27 February 2018 / Accepted: 1 March 2018 / Published: 6 March 2018
PDF Full-text (3840 KB) | HTML Full-text | XML Full-text | Supplementary Files
Abstract
The most common method for quantifying small-molecule drugs in blood samples is by liquid chromatography in combination with mass spectrometry. Few immuno-based assays are available for the detection of small-molecule drugs in blood. Here we report on a homogeneous assay that enables detection [...] Read more.
The most common method for quantifying small-molecule drugs in blood samples is by liquid chromatography in combination with mass spectrometry. Few immuno-based assays are available for the detection of small-molecule drugs in blood. Here we report on a homogeneous assay that enables detection of the concentration of digoxin spiked into in a plasma sample. The assay is based on a shift in the equilibrium of a DNA strand displacement competition reaction, and can be performed in 30 min for concentrations above 10 nM. The equilibrium shift occurs upon binding of anti-digoxigenin antibody. As a model, the assay provides a potential alternative to current small-molecule detection methods used for therapeutic drug monitoring. Full article
(This article belongs to the Special Issue FRET-Based Biosensors)
Figures

Figure 1

Review

Jump to: Research

Open AccessFeature PaperReview
Homotransfer FRET Reporters for Live Cell Imaging
Biosensors 2018, 8(4), 89; https://doi.org/10.3390/bios8040089
Received: 6 September 2018 / Revised: 27 September 2018 / Accepted: 10 October 2018 / Published: 11 October 2018
PDF Full-text (853 KB) | HTML Full-text | XML Full-text
Abstract
Förster resonance energy transfer (FRET) between fluorophores of the same species was recognized in the early to mid-1900s, well before modern heterotransfer applications. Recently, homotransfer FRET principles have re-emerged in biosensors that incorporate genetically encoded fluorescent proteins. Homotransfer offers distinct advantages over the [...] Read more.
Förster resonance energy transfer (FRET) between fluorophores of the same species was recognized in the early to mid-1900s, well before modern heterotransfer applications. Recently, homotransfer FRET principles have re-emerged in biosensors that incorporate genetically encoded fluorescent proteins. Homotransfer offers distinct advantages over the standard heterotransfer FRET method, some of which are related to the use of fluorescence polarization microscopy to quantify FRET between two fluorophores of identical color. These include enhanced signal-to-noise, greater compatibility with other optical sensors and modulators, and new design strategies based upon the clustering or dimerization of singly-labeled sensors. Here, we discuss the theoretical basis for measuring homotransfer using polarization microscopy, procedures for data collection and processing, and we review the existing genetically-encoded homotransfer biosensors. Full article
(This article belongs to the Special Issue FRET-Based Biosensors)
Figures

Figure 1

Biosensors EISSN 2079-6374 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top