Heavy atom induced phosphorescence study on the influence of internal structural factors on the photophysics of tryptophan in aqueous solutions.
In this study the effect of alanyl residue insertion into tryptophan and to some extent the effect of peptide bond on the photophysics of tryptophan chromophore has been studied. The photophysical parameters crucial in triplet state decay mechanism of aqueous AW, WA and AWA peptides have been determined applying our previously proposed methodology based on the heavy atom effect and compared with the previously reported values for tryptophan (Kowalska-Baron et al., 2012). The obtained results clearly indicated that the presence of alanyl residue and the peptide bond results in the changes in the fluorescence and phosphorescence decay kinetics of tryptophan. The fluorescence decays of the oligopeptides studied at pH 7 were biexponential. The longer lifetime component of WA arises from anionic form of this dipeptide, while the shorter one may be assigned to the zwitterionic form of WA. The observed invariance of the lifetimes of anionic and zwitterionic forms of WA throughout the pH studied supports the idea that these two components of WA fluorescence decay correspond to nearly independent species, possibly interconverting but at a rate slower than the fluorescence decay rates. Comparing the determined phosphorescence spectra of the oligopeptides studied with that of tryptophan, a slight blue-shift and more evident red-shift was observed in the spectrum of AW and WA, respectively. On the basis of the results of the phosphorescence measurements performed at pH 10, the 170 μs lifetime of WA, observed even at pH 7, may be assigned to the anionic form of the compound. It may be suggested that at pH 7 during the excited triplet state lifetime of WA there is a shift in the equilibrium towards the anionic form of this dipeptide. In the case of AW and AWA at pH 7 the obtained monoexponential decay kinetics, most probably, arise from zwitterionic forms of these peptides. The determined triplet quantum yield of AWA is slightly lower than that of tryptophan, while the quantum yield of AW is twofold lower than that of tryptophan. The highest value of the determined triplet quantum yield of WA confirms the presence of anionic form of this dipeptide at pH 7.
Institute of General Food Chemistry, Faculty of Biotechnology and Food Sciences, Technical University of Lodz, ul. Stefanowskiego 4/10, 90-924 Lodz, Poland. Electronic address: agnieszka.kowalska-baron@p.lodz.pl.
Agnieszka
A
Kowalska-Baron
Institute of General Food Chemistry, Faculty of Biotechnology and Food Sciences, Technical University of Lodz, ul. Stefanowskiego 4/10, 90-924 Lodz, Poland.
Krystian
K
Gałęcki
Institute of Organic Chemistry, Technical University of Lodz, Lodz, Poland.
Kamil
K
Rożniakowski
Institute of Organic Chemistry, Technical University of Lodz, Lodz, Poland.
Beata
B
Kolesińska
Institute of Organic Chemistry, Technical University of Lodz, Lodz, Poland.
Zbigniew J
ZJ
Kamiński
Institute of General Food Chemistry, Faculty of Biotechnology and Food Sciences, Technical University of Lodz, ul. Stefanowskiego 4/10, 90-924 Lodz, Poland.
Stanisław
S
Wysocki
D000409:Alanine / Q000737:chemistry; D005453:Fluorescence; D006863:Hydrogen-Ion Concentration; D009842:Oligopeptides / Q000737:chemistry*; D014364:Tryptophan / Q000737:chemistry*
D009842:Oligopeptides; D014364:Tryptophan; D000409:Alanine
Iodide quenching; N- and C-terminal tryptophan dipeptides; Phosphorescence lifetime; Tryptophan