Photo-isomerization and oxidation of bilirubin in mammals is dependent on albumin binding

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11110%2F15%3A10312700" target="_blank" >RIV/00216208:11110/15:10312700 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/60461373:22340/15:43900288

Výsledek na webu

<a href="http://dx.doi.org/10.1016/j.ab.2015.08.001" target="_blank" >http://dx.doi.org/10.1016/j.ab.2015.08.001</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.ab.2015.08.001" target="_blank" >10.1016/j.ab.2015.08.001</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Photo-isomerization and oxidation of bilirubin in mammals is dependent on albumin binding

Popis výsledku v původním jazyce

The bilirubin (BR) photo-conversion in the human body is a protein-dependent process; an effective photo-isomerization of the potentially neurotoxic Z,Z-BR as well as its oxidation to biliverdin in the antioxidant redox cycle is possible only when BR isbound on serum albumin. We present a novel analytical concept in the study of linear tetrapyrroles metabolic processes based on an in-depth mapping of binding sites in the structure of human serum albumin (HSA). A combination of fluorescence spectroscopy, circular dichroism (CD) spectroscopy, and molecular modeling methods was used for recognition of the binding site for BR, its derivatives (mesobilirubin and bilirubin ditaurate), and the products of the photo-isomerization and oxidation (lumirubin, biliverdin, and xanthobilirubic acid) on HSA. The CD spectra and fluorescent quenching of the Trp-HSA were used to calculate the binding constants. The results of the CD displacement experiments performed with hemin were interpreted together

Název v anglickém jazyce

Photo-isomerization and oxidation of bilirubin in mammals is dependent on albumin binding

Popis výsledku anglicky

The bilirubin (BR) photo-conversion in the human body is a protein-dependent process; an effective photo-isomerization of the potentially neurotoxic Z,Z-BR as well as its oxidation to biliverdin in the antioxidant redox cycle is possible only when BR isbound on serum albumin. We present a novel analytical concept in the study of linear tetrapyrroles metabolic processes based on an in-depth mapping of binding sites in the structure of human serum albumin (HSA). A combination of fluorescence spectroscopy, circular dichroism (CD) spectroscopy, and molecular modeling methods was used for recognition of the binding site for BR, its derivatives (mesobilirubin and bilirubin ditaurate), and the products of the photo-isomerization and oxidation (lumirubin, biliverdin, and xanthobilirubic acid) on HSA. The CD spectra and fluorescent quenching of the Trp-HSA were used to calculate the binding constants. The results of the CD displacement experiments performed with hemin were interpreted together

Druh

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

CEP obor

CE - Biochemie

OECD FORD obor

—

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

S - Specificky vyzkum na vysokych skolach

Rok uplatnění

2015

Kód důvěrnosti údajů

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

Název periodika

Analytical Biochemistry

ISSN

0003-2697

e-ISSN

—

Svazek periodika

490

Číslo periodika v rámci svazku

December

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

12

Strana od-do

34-45

Kód UT WoS článku

000363360500006

EID výsledku v databázi Scopus

2-s2.0-84942322884