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

The result's identifiers

  • Result code in 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>

  • Alternative codes found

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

  • Result on the web

    <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>

Alternative languages

  • Result language

    angličtina

  • Original language name

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

  • Original language description

    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.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • OECD FORD branch

    10608 - Biochemistry and molecular biology

Result continuities

  • Project

    <a href="/en/project/GJ19-21237Y" target="_blank" >GJ19-21237Y: New electrochemical approaches for the study of modified fatty acids and their biomolecular interactions</a><br>

  • Continuities

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

Others

  • Publication year

    2022

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES

  • ISSN

    0141-8130

  • e-ISSN

    1879-0003

  • Volume of the periodical

    203

  • Issue of the periodical within the volume

    April 2022

  • Country of publishing house

    NL - THE KINGDOM OF THE NETHERLANDS

  • Number of pages

    14

  • Pages from-to

    116-129

  • UT code for WoS article

    000782122500005

  • EID of the result in the Scopus database

    2-s2.0-85123682526