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Inhibitory mechanism of sinapinic acid against peroxynitrite‐mediated tyrosine nitration of protein in vitro
Author(s) -
Niwa Toshio,
Doi Umeyuki,
Kato Yoji,
Osawa Toshihiko
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)01216-8
Subject(s) - chemistry , caffeic acid , peroxynitrite , chromatography , nitrotyrosine , dimer , organic chemistry , antioxidant , nitric oxide , enzyme , nitric oxide synthase , superoxide
The peroxynitrite‐scavenging ability of some phenolic antioxidants, p ‐coumaric acid, caffeic acid and sinapinic acid, was examined and compared with ascorbic acid and tocopherol using 3‐nitrotyrosine formation as a marker. Among these, caffeic acid and sinapinic acid strongly inhibited the formation of 3‐nitrotyrosine in protein. The treatment of protein with peroxynitrite in the presence of sinapinic acid, but not caffeic acid, produced a novel product determined by reversed‐phase high performance liquid chromatography (HPLC). The product formed was purified and then identified as a mono‐lactone type dimer (ML) of sinapinic acid by nuclear magnetic resonance (NMR) and liquid chromatography‐mass spectrometry (LC‐MS). This ML was converted from a di‐lactone type dimer, obtained from sinapinic acid with peroxidase/hydrogen peroxide, in neutral buffer. In this report, we have proposed that the ML of sinapinic acid is generated via one‐electron oxidation by peroxynitrite treatment.