Biochemical and Biophysical Research Communications 1996-02-15

Characterization of the fluorescence emission properties of 7-azatryptophan in reverse micellar environments.

J Guharay, P K Sengupta

Index: Biochem. Biophys. Res. Commun. 219(2) , 388-92, (1996)

Full Text: HTML

Abstract

The amino acid analogue 7-azatryptophan has attracted significant recent attention as a novel optical probe for protein structure, function and dynamics. We report here, for the first time, its fluorescence emission behavior in a membrane mimetic model system, namely reverse micelles of aerosol-OT in n-heptane, containing varying amounts of added H2O or D2O. Upon increase in the water/surfactant molar ratio from 0.5 to 50 the emission maximum undergoes a pronounced red shift (by 20 nm), which is accompanied by dramatic quenching of the fluorescence emission and sharp decrease in its average lifetime. These data are used to infer the microenvironments of the fluorophore in the reverse micelles. Furthermore, the highly sensitive dependence of the fluorescence emission parameters of 7-azatryptophan on the water content of the reverse micelles highlights its suitability as a probe for water restricted environments, with possible applications to interfacial regions of biomembranes.

Related Compounds

  • 7-azatryptophan

Related Articles:

Phosphorescence and optically detected magnetic resonance characterization of the environments of tryptophan analogues in staphylococcal nuclease, its V66W mutant, and Delta 137-149 fragment.

1998-06-23

[Biochemistry 37(25) , 8954-64, (1998)]

Blue fluorescent amino acids as in vivo building blocks for proteins.

2010-02-15

[ChemBioChem. 11(3) , 305-14, (2010)]

In vivo properties of thiol inhibitors of the three vasopeptidases NEP, ACE and ECE are improved by introduction of a 7-azatryptophan in P2' position.

2004-02-01

[J. Pept. Res. 63(2) , 99-107, (2004)]

Biosynthetic incorporation of tryptophan analogues into staphylococcal nuclease: effect of 5-hydroxytryptophan and 7-azatryptophan on structure and stability.

1997-03-01

[Protein Sci. 6(3) , 689-97, (1997)]

Incorporation of the fluorescent amino acid 7-azatryptophan into the core domain 1-47 of hirudin as a probe of hirudin folding and thrombin recognition.

2004-06-01

[Protein Sci. 13(6) , 1489-502, (2004)]

More Articles...