Fret-flim Analysis

FRET-FLIM analysis is a fluorescence microscopy method that detects molecular interactions and conformational changes by combining Förster resonance energy transfer with fluorescence lifetime imaging. When a fluorescent donor and acceptor approach within nanometer-scale proximity, energy transfer reduces the donor’s fluorescence lifetime, which FLIM measures from the time-resolved decay of emitted light rather than signal intensity alone. In immunology and infection research, this approach can reveal receptor engagement, immune-signaling events, protein organization, and interactions between host and pathogen molecules in living cells. These measurements help connect molecular proximity with cellular responses and clarify mechanisms of infection, immunity, and therapeutic action.

Fret-flim Analysis - Related Videos

Research

JoVE EoE - Biomolecular Interaction Detection Techniques

FLIM-FRET Imaging for Characterization of Protein-Protein Interactions in Live Bacteria

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2025

The video describes the FLIM-FRET imaging technique to determine the protein-protein interaction in live bacteria expressing cytoplasmic proteins labeled with fluorescent proteins, a donor eGFP, and acceptor mCherry. The combined technique also allows the quantification of the interacting proteins.

FLIM-FRET Measurements of Protein-Protein Interactions in Live Bacteria.

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Cited by 7 •

2020

We describe here a protocol to characterize protein-protein interactions between two highly-differently expressed proteins in live Pseudomonas aeruginosa using FLIM-FRET measurements. The protocol includes bacteria strain constructions, bacteria immobilization, imaging and post-imaging data analysis routines.

Research

JoVE Journal - Biology
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FRET Imaging in Three-dimensional Hydrogels

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Cited by 3 •

2016

Förster resonance energy transfer (FRET) imaging is a powerful tool for real-time cell biology studies. Here a method for FRET imaging cells in physiologic three-dimensional (3D) hydrogel microenvironments using conventional epifluorescence microscopy is presented. An analysis for ratiometric FRET probes that yields linear ratios over the activation range is described.

Education

JoVE Science Education - Chemistry

Förster Resonance Energy Transfer (FRET)

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2023

Förster resonance energy transfer (FRET) is a phenomenon used to investigate close-range biochemical interactions. In FRET, a donor photoluminescent molecule can non-radiatively transfer energy to an acceptor molecule if their respective emission and absorbance spectra overlap. The amount of energy transferred—and consequently the overall emission of sample—depends on the proximity of an acceptor-donor pair of photoluminescent molecules. FRET analysis is combined with other biochemistry...

Quantitative FRET (Förster Resonance Energy Transfer) Analysis for SENP1 Protease Kinetics Determination

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Cited by 7 •

2013

A novel method involving quantitative analysis of FRET (Förster Resonance Energy Transfer) signals is described for studying enzyme kinetics. KM and kcat were obtained for the hydrolysis of the catalytic domain of SENP1 (SUMO/Sentrin specific protease 1) to pre-SUMO1 (Small Ubiquitin-like MOdifier). The general principles of this quantitative-FRET-based protease kinetic study can be applied to other proteases.

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