Serum albumin as a primary non-covalent binding protein for nitro-oleic acid

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15110%2F22%3A73614970" target="_blank" >RIV/61989592:15110/22:73614970 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/61989592:15310/22:73614970 RIV/00209805:_____/22:00078944

Výsledek na webu

<a href="https://www.sciencedirect.com/science/article/pii/S0141813022000605?via%3Dihub" target="_blank" >https://www.sciencedirect.com/science/article/pii/S0141813022000605?via%3Dihub</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.ijbiomac.2022.01.050" target="_blank" >10.1016/j.ijbiomac.2022.01.050</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Serum albumin as a primary non-covalent binding protein for nitro-oleic acid

Popis výsledku v původním jazyce

This work explores the interaction of 9/10-nitro-oleic acid (NO2-OA) with human serum albumin (HSA). The molecular mechanism of the biological action of NO2-OA is to our knowledge based on a reversible covalent reaction-Michael addition of nucleophilic amino acid residues of proteins. Since HSA is an important fatty acid transporter, a key question is whether NO2-OA can bind covalently or non-covalently to HSA, similarly to oleic acid (OA), which can interact with the FA1-FA7 binding sites of the HSA molecule. 1H NMR studies and competition analysis with OA and the drugs ibuprofen and warfarin were used to investigate a potential non-covalent binding mode. NO2-OA/HSA binding was confirmed to compete with warfarin for FA-7 with significantly higher affinity. NO2-OA competes with ibuprofen for FA-3 and FA-6, however, in contrast to the situation with warfarin, the binding affinities are not significantly different. The described interactions are based exclusively on non-covalent binding. No covalent binding of NO2-OA to HSA was detected by MS/MS. More detailed studies based on MALDI-TOF-MS and Ellman&apos;s assay indicated that HSA can be covalently modified in the presence of NO2-OA to a very limited extent. It was also shown that NO2-OA has a higher affinity to HSA than that of OA.

Název v anglickém jazyce

Serum albumin as a primary non-covalent binding protein for nitro-oleic acid

Popis výsledku anglicky

This work explores the interaction of 9/10-nitro-oleic acid (NO2-OA) with human serum albumin (HSA). The molecular mechanism of the biological action of NO2-OA is to our knowledge based on a reversible covalent reaction-Michael addition of nucleophilic amino acid residues of proteins. Since HSA is an important fatty acid transporter, a key question is whether NO2-OA can bind covalently or non-covalently to HSA, similarly to oleic acid (OA), which can interact with the FA1-FA7 binding sites of the HSA molecule. 1H NMR studies and competition analysis with OA and the drugs ibuprofen and warfarin were used to investigate a potential non-covalent binding mode. NO2-OA/HSA binding was confirmed to compete with warfarin for FA-7 with significantly higher affinity. NO2-OA competes with ibuprofen for FA-3 and FA-6, however, in contrast to the situation with warfarin, the binding affinities are not significantly different. The described interactions are based exclusively on non-covalent binding. No covalent binding of NO2-OA to HSA was detected by MS/MS. More detailed studies based on MALDI-TOF-MS and Ellman&apos;s assay indicated that HSA can be covalently modified in the presence of NO2-OA to a very limited extent. It was also shown that NO2-OA has a higher affinity to HSA than that of OA.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10608 - Biochemistry and molecular biology

Projekt

<a href="/cs/project/GJ19-21237Y" target="_blank" >GJ19-21237Y: Nové elektrochemické přístupy pro studium modifikovaných mastných kyselin a jejich biomolekulárních interakcí</a><br>

Návaznosti

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

Rok uplatnění

2022

Kód důvěrnosti údajů

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

Název periodika

INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES

ISSN

0141-8130

e-ISSN

1879-0003

Svazek periodika

203

Číslo periodika v rámci svazku

April 2022

Stát vydavatele periodika

NL - Nizozemsko

Počet stran výsledku

14

Strana od-do

116-129

Kód UT WoS článku

000782122500005

EID výsledku v databázi Scopus

2-s2.0-85123682526