Autor: Hernychová, L.; Alexandri, E.; Tzakos, A. G.; Zatloukalová, M.; Primikyri, A.; Gerothanassis, I. P.; Uhrik, L.; Šebela, M.; Kopečný, D.; Jedinák, L.; Vacek, J.
Název práce v češtině: Sérový albumin jako primární nekovalentní vazebný protein nitroolejové kyseliny
Název práce v angličtině: Serum albumin as a primary non-covalent binding protein for nitro-oleic acid
Studentská publikace: ne
Klíčová slova v češtině: addukce, nitro-mastné kyseliny, nekovalentní interakce, olejová kyselina, redukovaný albumin, sérový albumin
Klíčová slova v angličtině: Adduction, Nitro-fatty acid, Non-covalent interaction, Oleic acid, Reduced albumin, Serum albumin
Abstrakt česky: Práce zkoumá interakci 9/10-nitroolejové kyseliny (NO2OA) s lidským sérovým albuminem (HSA). Molekulární mechanismus je založen na reversibilní kovalentní reakci Miachelovy adice nukleofilních amino kyselinových zbytků proteinů.
Abstrakt 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’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.
Jazyk v originále: angličtina
Název časopisu: Int. J. Biol. Macromol.
Rok: 2022
Svazek (ročník): 2022 (203)
Číslo časopisu v rámci uvedeného svazku: 4
Strana od-do: 116-129
Impact factor: 8.025
Q1: ne

ISSN časopisu: 0141-8130
Vydavatel: Elsevier
Způsob financování: GJ19-21237Y
DOI: 10.1016/j.ijbiomac.2022.01.050