Fluorescence lifetime imaging – techniques and applications
Abstract
Summary: Fluorescence lifetime imaging (FLIM) uses the fact that the fluorescence lifetime of a fluorophore depends on its molecular environment but not on its concentration. Molecular effects in a sample can therefore be investigated independently of the variable, and usually unknown concentration of the fluorophore. There is a variety of technical solutions of lifetime imaging in microscopy. The technical part of this paper focuses on time‐domain FLIM by multidimensional time‐correlated single photon counting, time‐domain FLIM by gated image intensifiers, frequency‐domain FLIM by gain‐modulated image intensifiers, and frequency‐domain FLIM by gain‐modulated photomultipliers. The application part describes the most frequent FLIM applications: Measurement of molecular environment parameters, protein‐interaction measurements by Förster resonance energy transfer (FRET), and measurements of the metabolic state of cells and tissue via their autofluorescence. Measurements of local environment parameters are based on lifetime changes induced by fluorescence quenching or conformation changes of the fluorophores. The advantage over intensity‐based measurements is that no special ratiometric fluorophores are needed. Therefore, a much wider selection of fluorescence markers can be used, and a wider range of cell parameters is accessible. FLIM‐FRET measures the change in the decay function of the FRET donor on interaction with an acceptor. FLIM‐based FRET measurement does not have to cope with problems like donor bleedthrough or directly excited acceptor fluorescence. This relaxes the requirements to the absorption and emission spectra of the donors and acceptors used. Moreover, FLIM‐FRET measurements are able to distinguish interacting and noninteracting fractions of the donor, and thus obtain independent information about distances and interacting and noninteracting protein fractions. This is information not accessible by steady‐state FRET techniques. Autofluorescence FLIM exploits changes in the decay parameters of endogenous fluorophores with the metabolic state of the cells or the tissue. By resolving changes in the binding, conformation, and composition of biologically relevant compounds FLIM delivers information not accessible by steady‐state fluorescence techniques.
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Self-citationA Cellular Screening Assay Using Analysis of Metal-Modified Fluorescence Lifetime
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Ritman-Meer, T., Cade, N. I., & Richards, D. R. (2007) · Applied Physics Letters · doi:10.1063/1.2789700 · Cited by 27 · see citing works
(2008) · Springer eBooks · doi:10.1007/978-3-540-79401-1_4 · Cited by 27 · see citing works
How fast can TCSPC FLIM be made?
Katsoulidou, V., Bergmann, A., & Becker, W. H. (2007) · Proceedings of SPIE, the International Society for Optical Engineering/Proceedings of SPIE · doi:10.1117/12.735550 · Cited by 26 · see citing works
Self-citationSurvey of Endogenous Biological Fluorophores
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Fast-acquisition multispectral FLIM by parallel TCSPC
Becker, W. H., Su, B., & Bergmann, A. (2009) · Proceedings of SPIE, the International Society for Optical Engineering/Proceedings of SPIE · doi:10.1117/12.807697 · Cited by 19 · see citing works
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Becker, W. H., Bergmann, A., Haustein, E., et al. (2005) · Proceedings of SPIE, the International Society for Optical Engineering/Proceedings of SPIE · doi:10.1117/12.588990 · Cited by 19 · see citing works
Self-citationPetrášek, Z., & Suhling, K. (2010) · Optics Express · doi:10.1364/oe.18.024888 · Cited by 18 · see citing works
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Becker, W. H., Su, B., & Bergmann, A. (2012) · Proceedings of SPIE, the International Society for Optical Engineering/Proceedings of SPIE · doi:10.1117/12.908663 · Cited by 6 · see citing works
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Kemnitz, K. (2001) · Springer series on fluorescence · doi:10.1007/978-3-642-56853-4_18 · Cited by 3 · see citing works
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- Authors
- BECKER, W.
- Corresponding author
- BECKER, W.
- ORCID
- BECKER, W.
- Venue
- Journal of Microscopy
- Publisher
- Wiley
- Published
- 2012-05-24
- Volume
- 247
- Issue
- 2
- Pages
- 119-136
- ISSN
- 0022-2720 (ISSN-L)
- 1365-2818
- OpenAlex
- W1960176772
- Cited by
- 890
- References
- 126
- Citations by year
- 2026: 58 · 2025: 90 · 2024: 84 · 2023: 69 · 2022: 51 · 2021: 65 · 2020: 74 · 2019: 93 · 2018: 68 · 2017: 55 · 2016: 47 · 2015: 50 · 2014: 49 · 2013: 32 · 2012: 3
- FWCI
- 5.27
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Journal of Microscopy (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biophysics › Advanced Fluorescence Microscopy Techniques
- Physical Sciences › Chemistry › Physical and Theoretical Chemistry › Photochemistry and Electron Transfer Studies
- Health Sciences › Medicine › Radiology, Nuclear Medicine and Imaging › Optical Imaging and Spectroscopy Techniques
- Keywords
- fluorescence lifetime imaging, time-correlated single photon counting, fluorescence resonance energy transfer, FLIM-FRET, fluorescence quenching, protein-protein interaction, tissue autofluorescence, endogenous fluorophores, molecular environment
- MeSH terms
- Image Processing, Computer-Assisted, Microscopy, Fluorescence
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
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