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Serum albumin as a primary non-covalent binding protein for nitro-oleic acid
L. Hernychova, E. Alexandri, AG. Tzakos, M. Zatloukalová, A. Primikyri, IP. Gerothanassis, L. Uhrik, M. Šebela, D. Kopečný, L. Jedinák, J. Vacek
Jazyk angličtina Země Nizozemsko
Typ dokumentu časopisecké články
Odkazy
PubMed
35063491
DOI
10.1016/j.ijbiomac.2022.01.050
Knihovny.cz E-zdroje
- MeSH
- dusíkaté sloučeniny MeSH
- kyselina olejová MeSH
- kyseliny olejové MeSH
- lidé MeSH
- sérový albumin * chemie MeSH
- tandemová hmotnostní spektrometrie MeSH
- transportní proteiny * metabolismus MeSH
- vazba proteinů MeSH
- Check Tag
- lidé MeSH
- Publikační typ
- časopisecké články MeSH
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'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.
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- $a Hernychova, Lenka $u Research Centre for Applied Molecular Oncology, Masaryk Memorial Cancer Institute, Žlutý kopec 7, Brno 656 53, Czech Republic
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- $a 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'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.
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- $a Alexandri, Eleni $u Section of Organic Chemistry and Biochemistry, Department of Chemistry, University of Ioannina, Ioannina 451 10, Greece
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- $a Zatloukalová, Martina $u Department of Medical Chemistry and Biochemistry, Faculty of Medicine and Dentistry, Palacký University, Hněvotínská 3, Olomouc 775 15, Czech Republic
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- $a Šebela, Marek $u Department of Biochemistry, Faculty of Science, Palacký University, Šlechtitelů 27, Olomouc 783 71, Czech Republic
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- $a Kopečný, David $u Department of Experimental Biology, Faculty of Science, Palacký University, Šlechtitelů 27, Olomouc 783 71, Czech Republic
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- $a Jedinák, Lukáš $u Department of Organic Chemistry, Faculty of Science, Palacký University, 17. listopadu 12, Olomouc 771 46, Czech Republic
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- $a Vacek, Jan $u Department of Medical Chemistry and Biochemistry, Faculty of Medicine and Dentistry, Palacký University, Hněvotínská 3, Olomouc 775 15, Czech Republic; The Czech Academy of Sciences, Institute of Biophysics, Královopolská 135, Brno 612 65, Czech Republic. Electronic address: jan.vacek@upol.cz
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