AI Article Synopsis
- Laurdan is a fluorescent probe that is highly sensitive to the polarity and dynamics of its surroundings, particularly in biological membranes, reflecting these changes through significant spectral shifts.
- Steady-state measurements of Laurdan's general polarization (GP) indicate low water content in areas where there’s little molecular relaxation, highlighting its role in analyzing membrane characteristics.
- Additionally, Laurdan can act as a Förster-type resonance energy transfer (FRET) acceptor for tryptophan, allowing researchers to study lipid states near tryptophan residues in membrane proteins, such as the nicotinic acetylcholine receptor.
Article Abstract
The extrinsic fluorescent probe Laurdan (6-dodecanoyl-2-dimethylamino naphthalene) exhibits extreme sensitivity to the polarity and to the molecular dynamics of the dipoles in its environment. Dipolar relaxation processes are reflected as relatively large spectral shifts. Steady-state measurements of the so-called general polarization (GP) of Laurdan exploit the advantageous spectral properties of Laurdan. Since the main solvent dipoles surrounding Laurdan in biological membranes are water molecules, when no relaxation occurs GP values are high, indicating low water content in the hydrophilic/hydrophobic interface region. Laurdan fluorescence can also be used to obtain topographical information. A hitherto unexploited property of Laurdan, namely its ability to act as a Förster-type resonance energy transfer (FRET) acceptor of tryptophan emission, was used to learn about the physical state of lipids within Förster distance from donor tryptophan residues in integral membrane proteins. The application of this technique to the paradigm integral membrane protein, the nicotinic acetylcholine receptor, is described in this chapter.
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| http://dx.doi.org/10.1007/978-1-59745-519-0_36 | DOI Listing |
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