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Pressure effects on tryptophan and its derivatives
1Shanghai Institute of Biochemistry Academia Sinica, 320, Yue-Yang Road, Shanghai, 200031, China.
Biochemical and Biophysical Research Communications
|March 18, 2000
Summary
High pressure alters tryptophan fluorescence spectra, shifting them towards red. Fluorescence efficiency decreases with pressure, except for free tryptophan, necessitating consideration in biomolecular studies.
Area of Science:
- Biophysics
- Spectroscopy
Background:
- Tryptophan fluorescence is a common probe for protein structure.
- Understanding pressure effects on tryptophan is crucial for interpreting biomolecular behavior under high pressure.
Purpose of the Study:
- To investigate the effects of high pressure on the fluorescence of tryptophan and its derivatives.
- To analyze spectral shifts and changes in fluorescence efficiency under pressures up to 650 MPa.
Main Methods:
- Spectroscopic analysis of tryptophan (Trp), N-acetyl-tryptophan (AT), N-acetyl-tryptophanamide (NATA), tryptophanamide (TA), and polypeptides.
- Measurement of fluorescence spectra center of mass (300-450 nm) and quantum yield under varying pressures (0.1-650 MPa).
Main Results:
- High pressure caused a red shift in fluorescence spectra for all studied compounds.
- Fluorescence efficiency decreased with pressure, except for free tryptophan, which showed enhancement.
- Glycerol, ethanol, and pH significantly influenced these pressure-dependent fluorescence changes.
Conclusions:
- Intrinsic pressure effects on tryptophan fluorescence must be considered when studying biomolecules under high pressure using fluorospectroscopic methods.
- The study explored and discussed the mechanisms behind these pressure-induced fluorescence alterations.