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This work is devoted to study how immobilization in the PVA films affects the fluorescence and phosphorescence lifetime of indole and its derivatives. The obtained results indicated that immobilization of the studied indoles in the PVA matrix, which leads to the increased microrigidity of the environment around the indole moiety, results in the increase of singlet and triplet excited state lifetime of the studied compounds. Most probably, the enhancement of the rigidity of the environment near the chromophore reduces the rates of the non-radiative deactivation pathways, which leads to the increase of excited state lifetimes of the studied compounds.
Czasopismo
Rocznik
Tom
Strony
3--14
Opis fizyczny
Bibliogr. 25 poz.
Twórcy
autor
autor
autor
- Institute of General Food Chemistry, Faculty of Biotechnology and Food Science, Technical University of Lodz, 90-924 Lodz, Poland, agnieszka.kowalska-baron@p.lodz.pl
Bibliografia
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- 3. Millar DP. Time-resolved fluorescence spectroscopy. Curr Opin Struct Biol 1996, 6:637-642.
- 4. Strambini EG, Strambini GB, Tryptophan phosphorescence as a monitor of protein conformations in molecular films. Biosens Bioelectron 2000, 15:483-490.
- 5. Strambini GB, Gonnelli M, Tryptophan phosphorescence in fluid solution. J Am Chem Soc 1995, 117:7646-7651.
- 6. Strambini GB., Kerwin BA, Mason BD. Gonelli M, The triplet-state lifetime of indole derivatives in aqueous solution. Photochem Photobiol 2004, 80:462-470.
- 7. Fischer CJ, Gafni A, Steel DG, Schauerte JA, The triplet-state lifetime of indole in aqueous and viscous environments: significance to the interpretation of room temperature phosphorescence in proteins. J Am Chem Soc 2002, 124:10359-10366.
- 8. Bent DV, Hayon E, Excited state chemistry of aromatic amino acids and related peptides. III. Tryptophan. J Am Chem Soc 1975, 97:2612-2619.
- 9. Tsentalowich Y, Snytnikova OA, Sagdeev RZ, Properties of excited states of aqueous tryptophan. J Photochem Photobiol A Chem 2004, 162:371-379.
- 10. Strambini GB, Gonnelli M. Tryptophan phosphorescence in fluid solutions. J Am Chem Soc 1995, 117:7646-7651.
- 11. Banks DD, Kerwin BA, A deoxygenation system for measuring protein phosphorescence. Anal Biochem 2004, 324:106-114.
- 12. Strambini GB, Gonelli M, The indole nucleus triplet-state lifetime and its dependence on solvent microviscosity. Chem Phys Lett 1985, 115:196-204.
- 13. Dashnau JL, Zelent B, Vanderkooi JM, Tryptophan interactions with glycerol/ water and trehalose/sucrose cryosolvents: infrared and fluorescence spectroscopy and ab initio calculations. Biophys Chem 2005, 114:71-83.
- 14. Rung-Shu C, Yi-Jane C, Min-Huey C, Tai-Horng Y, The behavior of rat tooth germ cells on poly(vinyl alcohol). Act Biomater 2009, 5:1064-1074.
- 15. Kuijt J, Ariese F, Brinkman UAT, Gooijer C, Room temperature phosphorescence in the liquid state as a tool in analytical chemistry. Anal Chim Acta 2003, 488:135-171.
- 16. Williams ATR., Winfield SA, Miller JN, Relative fluorescence quantum yields using a computer controlled luminescence spectrometer. Analyst 1983, 108:1067-1068.
- 17. Somers KRF, Kryachko ES, Ceulemans A, Theoretical study of indole: protonation, indolyl radical, tautomers of indole, and its interaction with water. Chem Phys 2004, 301:61-79.
- 18. Kamath SD, Kartha VB, Mahato KK, Dynamics of L-tryptophan in aqueous solution by simultaneous laser induced fluorescence (LIF) and photoacoustic spectroscopy (PAS). Spectrochim Act A 2008, 70:187-19.
- 19. Ryuzi K, Dependence of photoionization quantum yield of indole and tryptophan in water on excitation wavelength. J Photochem Photobiol A 2007, 189:211-217.
- 20. Feng S, Zong W, Liu R, Chai J, Liu Y, Micro-environmental influences on the fluorescence of tryptophan. Spectrochim Act A, 2010, 76:142-145.
- 21. Sau AK, Mitra S, Steady state and picosecond time-resolved fluorescence studies on native, desulpho and deflavo xanthine oxidase. Biochim Biophys Act 2000, 1481:273-282.
- 22. Kirby EP, Steiner RF, The influence of solvent and temperature upon the fluorescence of indole derivatives. J Phys Chem 1970, 74:4480-4490.
- 23. Singh AK, Aruna RV, Fluorescence studies of tryptophan and tryptophan-retinol Shiff base in reverse micellar matrix. J Photochem Photobiol A 1995, 89:247-250.
- 24. Qiang L, Seeger S, Label-free detection of protein interactions using deep UV fluorescence lifetime microscopy. Anal Biochem 2007, 367:104-110.
- 25. Zelent B, Kuśba J, Gryczynski I, Johnson MJ, Lakowicz JR, Time-resolved and steady state fluorescence quenching of N-acetyl-L-tryptophanamide by acrylamide and iodide. Biophys Chem 1998, 73:53-75.
Typ dokumentu
Bibliografia
Identyfikator YADDA
bwmeta1.element.baztech-article-LOD7-0032-0051