Fluorescence lifetime imaging

Klaus Suhling; Liisa M. Hirvonen; James A. Levitt; Pei Hua Chung; Carolyn Tregidgo; Dmitri A. Rusakov; Kaiyu Zheng; Simon Ameer-Beg; Simon P. Poland; Simao Coelho; Robert Henderson; Nikola Krstajic

doi:10.1007/978-94-007-5052-4_13

Fluorescence lifetime imaging

Klaus Suhling, Liisa M. Hirvonen, James A. Levitt, Pei Hua Chung, Carolyn Tregidgo, Dmitri A. Rusakov, Kaiyu Zheng, Simon Ameer-Beg, Simon P. Poland, Simao Coelho, Robert Henderson, Nikola Krstajic

Research output: Chapter in Book/Report/Conference proceeding › Chapter

6 Citations (Scopus)

Abstract

Fluorescence lifetime imaging (FLIM) is a key fluorescence microscopy technique to map the environment and interaction of fluorescent probes. It can report on photophysical events that are difficult or impossible to observe by fluorescence intensity imaging, because FLIM is largely independent of the local fluorophore concentration and excitation intensity. Many FLIM applications relevant for biology concern the identification of Förster resonance energy transfer (FRET) to study protein interactions and conformational changes. In addition, FLIM has been used to image viscosity, temperature, pH, refractive index, and ion and oxygen concentrations, all at the cellular level. The basic principles and recent advances in the application of FLIM, FLIM instrumentation, molecular probe, and FLIM detector development will be discussed.

Original language	English
Title of host publication	Handbook of Photonics for Biomedical Engineering
Editors	Aaron Ho-Pui Ho, Donghyun Kim, Michael G. Somekh
Place of Publication	Dordrecht
Publisher	Springer
Pages	353-405
Number of pages	53
ISBN (Electronic)	9789400750524
ISBN (Print)	9789400750517
DOIs	https://doi.org/10.1007/978-94-007-5052-4_13
Publication status	Published - 2017

Keywords

Anisotropy
Fluorescence anisotropy imaging (FAIM)
Fluorescence enhancement
Fluorescence microscopy
Fluorescence spectroscopy
Förster resonance energy transfer (FRET)
Plasmonics
Time-correlated single-photon counting (TCSPC)
Time-resolved fluorescence anisotropy imaging (TR-FAIM)
Total internal reflection fluorescence (TIRF)

ASJC Scopus subject areas

General Biochemistry,Genetics and Molecular Biology
General Engineering
General Physics and Astronomy

Access to Document

10.1007/978-94-007-5052-4_13

Cite this

Suhling, K., Hirvonen, L. M., Levitt, J. A., Chung, P. H., Tregidgo, C., Rusakov, D. A., Zheng, K., Ameer-Beg, S., Poland, S. P., Coelho, S., Henderson, R., & Krstajic, N. (2017). Fluorescence lifetime imaging. In A. Ho-Pui Ho, D. Kim, & M. G. Somekh (Eds.), Handbook of Photonics for Biomedical Engineering (pp. 353-405). Springer . https://doi.org/10.1007/978-94-007-5052-4_13

@inbook{cb0957e556fa4d659ac9d1d380225f19,

title = "Fluorescence lifetime imaging",

abstract = "Fluorescence lifetime imaging (FLIM) is a key fluorescence microscopy technique to map the environment and interaction of fluorescent probes. It can report on photophysical events that are difficult or impossible to observe by fluorescence intensity imaging, because FLIM is largely independent of the local fluorophore concentration and excitation intensity. Many FLIM applications relevant for biology concern the identification of F{\"o}rster resonance energy transfer (FRET) to study protein interactions and conformational changes. In addition, FLIM has been used to image viscosity, temperature, pH, refractive index, and ion and oxygen concentrations, all at the cellular level. The basic principles and recent advances in the application of FLIM, FLIM instrumentation, molecular probe, and FLIM detector development will be discussed.",

keywords = "Anisotropy, Fluorescence anisotropy imaging (FAIM), Fluorescence enhancement, Fluorescence microscopy, Fluorescence spectroscopy, F{\"o}rster resonance energy transfer (FRET), Plasmonics, Time-correlated single-photon counting (TCSPC), Time-resolved fluorescence anisotropy imaging (TR-FAIM), Total internal reflection fluorescence (TIRF)",

author = "Klaus Suhling and Hirvonen, {Liisa M.} and Levitt, {James A.} and Chung, {Pei Hua} and Carolyn Tregidgo and Rusakov, {Dmitri A.} and Kaiyu Zheng and Simon Ameer-Beg and Poland, {Simon P.} and Simao Coelho and Robert Henderson and Nikola Krstajic",

year = "2017",

doi = "10.1007/978-94-007-5052-4_13",

language = "English",

isbn = "9789400750517",

pages = "353--405",

editor = "{Ho-Pui Ho}, Aaron and Donghyun Kim and Somekh, {Michael G.}",

booktitle = "Handbook of Photonics for Biomedical Engineering",

publisher = "Springer ",

}

TY - CHAP

T1 - Fluorescence lifetime imaging

AU - Suhling, Klaus

AU - Hirvonen, Liisa M.

AU - Levitt, James A.

AU - Chung, Pei Hua

AU - Tregidgo, Carolyn

AU - Rusakov, Dmitri A.

AU - Zheng, Kaiyu

AU - Ameer-Beg, Simon

AU - Poland, Simon P.

AU - Coelho, Simao

AU - Henderson, Robert

AU - Krstajic, Nikola

PY - 2017

Y1 - 2017

N2 - Fluorescence lifetime imaging (FLIM) is a key fluorescence microscopy technique to map the environment and interaction of fluorescent probes. It can report on photophysical events that are difficult or impossible to observe by fluorescence intensity imaging, because FLIM is largely independent of the local fluorophore concentration and excitation intensity. Many FLIM applications relevant for biology concern the identification of Förster resonance energy transfer (FRET) to study protein interactions and conformational changes. In addition, FLIM has been used to image viscosity, temperature, pH, refractive index, and ion and oxygen concentrations, all at the cellular level. The basic principles and recent advances in the application of FLIM, FLIM instrumentation, molecular probe, and FLIM detector development will be discussed.

AB - Fluorescence lifetime imaging (FLIM) is a key fluorescence microscopy technique to map the environment and interaction of fluorescent probes. It can report on photophysical events that are difficult or impossible to observe by fluorescence intensity imaging, because FLIM is largely independent of the local fluorophore concentration and excitation intensity. Many FLIM applications relevant for biology concern the identification of Förster resonance energy transfer (FRET) to study protein interactions and conformational changes. In addition, FLIM has been used to image viscosity, temperature, pH, refractive index, and ion and oxygen concentrations, all at the cellular level. The basic principles and recent advances in the application of FLIM, FLIM instrumentation, molecular probe, and FLIM detector development will be discussed.

KW - Anisotropy

KW - Fluorescence anisotropy imaging (FAIM)

KW - Fluorescence enhancement

KW - Fluorescence microscopy

KW - Fluorescence spectroscopy

KW - Förster resonance energy transfer (FRET)

KW - Plasmonics

KW - Time-correlated single-photon counting (TCSPC)

KW - Time-resolved fluorescence anisotropy imaging (TR-FAIM)

KW - Total internal reflection fluorescence (TIRF)

U2 - 10.1007/978-94-007-5052-4_13

DO - 10.1007/978-94-007-5052-4_13

M3 - Chapter

AN - SCOPUS:85034393737

SN - 9789400750517

SP - 353

EP - 405

BT - Handbook of Photonics for Biomedical Engineering

A2 - Ho-Pui Ho, Aaron

A2 - Kim, Donghyun

A2 - Somekh, Michael G.

PB - Springer

CY - Dordrecht

ER -

Fluorescence lifetime imaging

Abstract

Keywords

ASJC Scopus subject areas

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