Nonexponential fluorescence decay of aqueous tryptophan and two related peptides by picosecond spectroscopy

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Abstract
Time-resolved fluorescence spectroscopy of tryptophan and 2 related dipeptides, tryptophylalanine and alanyltryptophan, was carried out on the subnanosecond time scale by using picosecond exciting pulses at a wavelength of 264 nm. Detection was with an ultrafast streak camera coupled to an optical multichannel analyzer. The zwitterions of these molecules show a definite nonexponential fluorescence decay which can be analyzed in terms of 2 exponentials. The 2 decay rates increase strongly with increasing temperature, as does the weight of the faster component. In tryptophan at pH 11, where the amino group is deprotonated, there remains only a single temperature-dependent exponential. The results are interpreted in terms of 2 kinds of trapped conformers in the excited state that interconvert no quicker than the time scale of the fluorescence. A model is suggested in which the non-radiative processes in one conformer approximate those in the bare indole moiety. The nonradiative decay rate of the other conformer is substantially faster. It is believed that the process responsible for this fast decay is intramolecular electron transfer from the indole ring to the amino acid side chain. The predilection for this electron transfer depends on steric relationships as well as on the electron-attracting power of the carbonyl group. This picture is consistent with earlier fluorescence quantum yield results. A self-consistent picture emerges from the temporal and yield data that quantitatively explains most important facets of tryptophan photochemistry in aqueous solution.