Fluorescence of sanguinarine: spectral changes on interaction with amino acids.

Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15310%2F10%3A10212346" target="_blank" >RIV/61989592:15310/10:10212346 - isvavai.cz</a>
Alternative codes found
RIV/61989592:15110/10:10212346
Result on the web
—
DOI - Digital Object Identifier
—

Result language
angličtina
Original language name
Fluorescence of sanguinarine: spectral changes on interaction with amino acids.
Original language description
The quaternary isoquinoline alkaloid, sanguinarine (SG) exhibits a wide range of biological activities. This study examines spectral changes expected from SG binding to proteins. Fluorescence spectra of the cationic form of sanguinarine (SG+) are sensitive to environment polarity. On the other hand, spectra of the neutral form of sanguinarine, pseudobase (SGOH) and dihydrosanguinarine (DHSG, the first metabolite of SG) exhibit higher sensitivity to the ability of solvent to form a solute-to-solvent hydrogen bonds. Interaction with cysteine has been the only mode of SG binding to enzymes that has been considered so far. We have also detected interactions of SGOH, SG+ and DHSG with other amino acids. Moreover, we have demonstrated that spectral change analysis can aid investigation of SG/DHSG interactions with proteins and we were able to identify SG+-binding site on Na+/K+-ATPase.
Czech name
—
Czech description
—

Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
BO - Biophysics
OECD FORD branch
—

Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>Z - Vyzkumny zamer (s odkazem do CEZ)<br>S - Specificky vyzkum na vysokych skolach

Publication year
2010
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Similar results(10)