Fluorescence quenching study on the interaction of bases of nucleic acid with electron-accepting sensitizer and serum albumin containing electron-rich tryptophan residue

Fluorescence quenching study on the interaction of bases of nucleic acid with electron-accepting... Static and dynamic fluorescence quenchings of electron-accepting sensitizers including positive charged heterocyclics and neutral cyanoaromatics by bases of nucleic acid (NB) have been investigated. It was found that NB could act as effective electron donors to quench the fluorescence of electron-accepting sensitizers. The quenchings by diffusion-controlled rate coincide well with the static and dynamic Stern-Volmer correlation. On the other hand, the diffusion-controlled fluorescence quenchings of the tryptophan (TRP) residue in the protein enzymes, HSA and BSA, by electron-accepting NB reveal that photochemical dual-damage of protein enzyme and thymine (THM) occur upon u.v.-irradiation, which is characteristic of excitation wavelength-dependence. Therefore, the results illustrate that the lesion interactions of NB with electron-deficient sensitizers or electron-rich TRP fluorophore-containing protein enzymes originate mainly from PET-initiated processes in both cases. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Research on Chemical Intermediates Springer Journals

Fluorescence quenching study on the interaction of bases of nucleic acid with electron-accepting sensitizer and serum albumin containing electron-rich tryptophan residue

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Publisher
Springer Netherlands
Copyright
Copyright © 2000 by Springer
Subject
Chemistry; Catalysis; Physical Chemistry; Inorganic Chemistry
ISSN
0922-6168
eISSN
1568-5675
D.O.I.
10.1163/156856700X00642
Publisher site
See Article on Publisher Site

Abstract

Static and dynamic fluorescence quenchings of electron-accepting sensitizers including positive charged heterocyclics and neutral cyanoaromatics by bases of nucleic acid (NB) have been investigated. It was found that NB could act as effective electron donors to quench the fluorescence of electron-accepting sensitizers. The quenchings by diffusion-controlled rate coincide well with the static and dynamic Stern-Volmer correlation. On the other hand, the diffusion-controlled fluorescence quenchings of the tryptophan (TRP) residue in the protein enzymes, HSA and BSA, by electron-accepting NB reveal that photochemical dual-damage of protein enzyme and thymine (THM) occur upon u.v.-irradiation, which is characteristic of excitation wavelength-dependence. Therefore, the results illustrate that the lesion interactions of NB with electron-deficient sensitizers or electron-rich TRP fluorophore-containing protein enzymes originate mainly from PET-initiated processes in both cases.

Journal

Research on Chemical IntermediatesSpringer Journals

Published: Jul 7, 2009

References

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