Cookies Policy
X

This site uses cookies. By continuing to browse the site you are agreeing to our use of cookies.

I accept this policy

Find out more here

Fluorescence Quenching Study On the Interaction of Bases of Nucleic Acid With Electron-Accepting Sensitizer and Serum Albumin Containing Electron-Rich Tryptophan Residue

No metrics data to plot.
The attempt to load metrics for this article has failed.
The attempt to plot a graph for these metrics has failed.
The full text of this article is not currently available.

Brill’s MyBook program is exclusively available on BrillOnline Books and Journals. Students and scholars affiliated with an institution that has purchased a Brill E-Book on the BrillOnline platform automatically have access to the MyBook option for the title(s) acquired by the Library. Brill MyBook is a print-on-demand paperback copy which is sold at a favorably uniform low price.

This Article is currently unavailable for purchase.
Add to Favorites
You must be logged in to use this functionality

Cover image Placeholder

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 Stem-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.

Affiliations: 1: Department of Chemistry, Tongji University, Shanghai 200092, CHINA

10.1163/156856700X00642
/content/journals/10.1163/156856700x00642
dcterms_title,pub_keyword,dcterms_description,pub_author
10
5
Loading
Loading

Full text loading...

/content/journals/10.1163/156856700x00642
Loading

Data & Media loading...

http://brill.metastore.ingenta.com/content/journals/10.1163/156856700x00642
Loading

Article metrics loading...

/content/journals/10.1163/156856700x00642
2017-12-13

Sign-in

Can't access your account?
  • Key

  • Full access
  • Open Access
  • Partial/No accessInformation