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Chemical Compound Review:

SureCN3202823 2-acetamido-3-(1H-indol-3- yl)propanamide

Synonyms: IBS-L0037277, Oprea1_140599, AC1L1CPL, AC1Q5IWI, AR-1H6489, ...

Lakowicz, J.R. et al., Fabris, C. et al., Lakowicz, J.R. et al., Kuramitsu, S. et al., Lakowicz, J.R. et al., et al.

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High impact information on N-Acetyl-L-tryptophanamide

We used phase fluorometry to investigate the wavelength dependence of the fluorescence lifetimes of N-acetyl-L-tryptophanamide (NATA) in solvents of varying viscosity and the lifetimes of tryptophan in human serum albumin, melittin, and liver alcohol dehydrogenase [1].
Moreover, the boronated phthalocyanine exhibits a high photosensitizing efficiency against a model biological substrate, such as N-acetyl-L-tryptophanamide, and a singlet oxygen quantum yield of 0.53 in dimethylformamide [2].
N-acetyl-L-tryptophanamide and glucagon [3].
The performance of the complete system has been tested with single lifetime standards like p-terphenyl in cyclohexane or with N-acetyl-L-tryptophanamide in pH 7.5 buffer [4].
7. The tryptophyl fluorescence spectrum excited at 295 nm had an emission maximum at 340 nm and the quantum efficiency of recA protein relative to N-acetyl-L-tryptophanamide was determined to be 0.65 [5].

Associations of N-Acetyl-L-tryptophanamide with other chemical compounds

Control experiments were performed on mixtures of N-acetyl-L-tryptophanamide (NATA) and PPD, which demonstrate our ability to recover the spectra and decay times from two component mixtures [6].
In addition, we examined 6-propionyl-2-dimethylaminonaphthalene (PRODAN) and N-acetyl-L-tryptophanamide (NATA) in viscous solvents where the solvent relaxation times were comparable to the fluorescence lifetimes [7].
We examined the time-resolved and steady-state fluorescence quenching of N-acetyl-L-tryptophanamide (NATA) by acrylamide and iodide, over a range of viscosities in propylene glycol [8].

Analytical, diagnostic and therapeutic context of N-Acetyl-L-tryptophanamide

We demonstrate using N-acetyl-L-tryptophanamide in water that the method of frequency-domain fluorometry is capable of measuring correlation times as short as 50 ps [9].
The fluorescence and circular dichroism of proteins in reverse micelles: application to the photophysics of human serum albumin and N-acetyl-L-tryptophanamide [10].

References

Dipolar relaxation in proteins on the nanosecond timescale observed by wavelength-resolved phase fluorometry of tryptophan fluorescence. Lakowicz, J.R., Cherek, H. J. Biol. Chem. (1980) [Pubmed]
Photosensitizing properties of a boronated phthalocyanine: studies at the molecular and cellular level. Fabris, C., Jori, G., Giuntini, F., Roncucci, G. J. Photochem. Photobiol. B, Biol. (2001) [Pubmed]
Viscosity dependence of the solute quenching of the tryptophanyl fluorescence of proteins. Eftink, M.R., Hagaman, K.A. Biophys. Chem. (1986) [Pubmed]
A subnanosecond resolving spectrofluorimeter for the analysis of protein fluorescence kinetics. van Hoek, A., Vervoort, J., Visser, A.J. J. Biochem. Biophys. Methods (1983) [Pubmed]
A large-scale preparation and some physicochemical properties of recA protein. Kuramitsu, S., Hamaguchi, K., Ogawa, T., Ogawa, H. J. Biochem. (1981) [Pubmed]
Resolution of two emission spectra for tryptophan using frequency-domain phase-modulation spectra. Lakowicz, J.R., Jayaweera, R., Szmacinski, H., Wiczk, W. Photochem. Photobiol. (1989) [Pubmed]
Analysis of excited-state processes by phase-modulation fluorescence spectroscopy. Lakowicz, J.R., Balter, A. Biophys. Chem. (1982) [Pubmed]
Time-resolved and steady-state fluorescence quenching of N-acetyl-L-tryptophanamide by acrylamide and iodide. Zelent, B., Kuśba, J., Gryczynski, I., Johnson, M.L., Lakowicz, J.R. Biophys. Chem. (1998) [Pubmed]
Measurement of subnanosecond anisotropy decays of protein fluorescence using frequency-domain fluorometry. Lakowicz, J.R., Laczko, G., Gryczynski, I., Cherek, H. J. Biol. Chem. (1986) [Pubmed]
The fluorescence and circular dichroism of proteins in reverse micelles: application to the photophysics of human serum albumin and N-acetyl-L-tryptophanamide. Davis, D.M., McLoskey, D., Birch, D.J., Gellert, P.R., Kittlety, R.S., Swart, R.M. Biophys. Chem. (1996) [Pubmed]

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