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

Kód výsledku v 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>

Nalezeny alternativní kódy

RIV/61989592:15110/10:10212346

Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

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

Popis výsledku v původním jazyce

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.

Název v anglickém jazyce

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

Popis výsledku anglicky

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.

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

BO - Biofyzika

OECD FORD obor

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Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

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

Rok uplatnění

2010

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Physical Chemistry Chemical Physics

ISSN

1463-9076

e-ISSN

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Svazek periodika

12

Číslo periodika v rámci svazku

37

Stát vydavatele periodika

GB - Spojené království Velké Británie a Severního Irska

Počet stran výsledku

7

Strana od-do

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Kód UT WoS článku

000281726800019

EID výsledku v databázi Scopus

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