Circular dichroism study of the interaction between mutagens and bilirubin bound to different binding sites of serum albumins

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60461373%3A22340%2F14%3A43897030" target="_blank" >RIV/60461373:22340/14:43897030 - isvavai.cz</a>

Výsledek na webu

<a href="http://dx.doi.org/10.1016/j.saa.2014.01.139" target="_blank" >http://dx.doi.org/10.1016/j.saa.2014.01.139</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.saa.2014.01.139" target="_blank" >10.1016/j.saa.2014.01.139</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Circular dichroism study of the interaction between mutagens and bilirubin bound to different binding sites of serum albumins

Popis výsledku v původním jazyce

Although recent investigations have shown that bilirubin not only has a negative role in the organism but also exhibits significant antimutagenic properties, the mechanisms of interactions between bilirubin and mutagens are not clear. In this study, interaction between bilirubin bound to different binding sites of mammalian serum albumins with structural analogues of the mutagens 2-aminofluorene, 2,7-diaminofluorene and mutagen 2,4,7-trinitrofluorenone were investigated by circular dichroism and absorption spectroscopy. Homological human and bovine serum albumins were used as chiral matrices, which preferentially bind different conformers of bilirubin in the primary binding sites and make it observable by circular dichroism. These molecular systems approximated a real system for the study of mutagens in blood serum. Differences between the interaction of bilirubin bound to primary and to secondary binding sites of serum albumins with mutagens were shown. For bilirubin bound to secondar

Název v anglickém jazyce

Circular dichroism study of the interaction between mutagens and bilirubin bound to different binding sites of serum albumins

Popis výsledku anglicky

Although recent investigations have shown that bilirubin not only has a negative role in the organism but also exhibits significant antimutagenic properties, the mechanisms of interactions between bilirubin and mutagens are not clear. In this study, interaction between bilirubin bound to different binding sites of mammalian serum albumins with structural analogues of the mutagens 2-aminofluorene, 2,7-diaminofluorene and mutagen 2,4,7-trinitrofluorenone were investigated by circular dichroism and absorption spectroscopy. Homological human and bovine serum albumins were used as chiral matrices, which preferentially bind different conformers of bilirubin in the primary binding sites and make it observable by circular dichroism. These molecular systems approximated a real system for the study of mutagens in blood serum. Differences between the interaction of bilirubin bound to primary and to secondary binding sites of serum albumins with mutagens were shown. For bilirubin bound to secondar

Druh

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

CEP obor

CB - Analytická chemie, separace

OECD FORD obor

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Projekt

<a href="/cs/project/GAP206%2F11%2F0836" target="_blank" >GAP206/11/0836: Strukturní studie potencionálně bioaktivních komplexů žlučových barviv: Vztak k jejich ochranné funkci v organismech</a><br>

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2014

Kód důvěrnosti údajů

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

Název periodika

Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy

ISSN

1386-1425

e-ISSN

—

Svazek periodika

126

Číslo periodika v rámci svazku

neuvedeno

Stát vydavatele periodika

NL - Nizozemsko

Počet stran výsledku

8

Strana od-do

68-75

Kód UT WoS článku

000335618200010

EID výsledku v databázi Scopus

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