Forster resonance energy transfer fluorophores

The lifetime of the excited state of fluorophores may be altered by physical and biochemical properties of its environment. Fluorescence lifetime imaging microscopy (FLIM) is thus a powerful analytical tool for the quantitative mapping of fluorescent molecules that reports, for instance, on local ion concentration, pH, and viscosity, the fluorescence lifetime of a donor fluorophore, Forster resonance energy transfer can be also imaged by FLIM. This provides a robust method for mapping protein-protein interactions and for probing the complexity of molecular interaction networks. 

Fluorescence or Forster resonance energy transfer (FRET) is widely accepted as being one of the most useful methods to observe biochemical events in vitro and in living cells. Generally, there are two forms of FRET sensors those based on a pair of genetically encoded fluorophores, usually employing fluorescent proteins from jellyfish or corals, or those based on small molecules that make use of small organic fluorophores. 

Forster resonance energy transfer (FRET) is a form of quenching. For a fluorophore (donor) to be quenched by another molecule (acceptor), three criteria must be met ... 

Clapp, A. R. Medintz, I. L. Mattoussi, H., Forster resonance energy transfer investigations using quantum dot fluorophores, Chemphyschem 2006, 7, 47 57... 

More sophisticated designs involved semiconductor quantum dots with fluorescent protein receptors immobilized on the surface [146], The binding site of the protein receptor is occupied with an efficient fluorophore. On excitation a series of FRET (Forster resonant energy transfer) processes takes place excitation energy is transferred from the core of the quantum dot to the fluorescent protein and subsequently to the fluorophore. On substrate binding only one FRET step takes place and luminescence of the receptor is observed [146], In the simplest sensor architecture the protein contains bound quencher. Upon interaction with analyte the quencher is liberated and luminescence of the quantum dot is observed (Figure 16.25c). 

In the case of Forster resonance energy transfer (FRET) [13], i.e. energy transfer by the dipole-dipole mechanism, and for randomly oriented donor-acceptor pairs, the depolarization after one transfer step (ensemble average) is almost complete [27]. For this reason, fluorescence anisotropy is a good indicator of energy transfer between identical fluorophores, hence of relative distances. Existence of efficient FRET may therefore reflect an association process. 

In fluorescence resonance energy transfer, also called Forster resonance energy transfer FRET), an excited fluorophore in one part of a molecule (the donor) has its fluorescence... 

Fluorescence resonance energy transfer (FRET), a phenomenon first described by Forster in 1948 [27], involves dipole-dipole energy transfer from the emitting fluorophore moiety (donor) to the absorbing moiety (acceptor). The rate of energy transfer (kx) for any specific donor (D) and acceptor (A) pair is given by... 

Forster energy transfer or energy transfer at a distance occurs between two molecules, a donor (the excited fluorophore), and an acceptor (a chromophore or fluorophore). Energy is transferred by resonance, i.e., the electron of the excited molecule induces an oscillating electric field that excites the acceptor electrons. As a result of this energy transfer, the fluorescence intensity and quantum yield of the emitter will decrease. Energy transfer is described in Chapter 14. 

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