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Imidazole dipeptides can quench toxic 4‐oxo‐2( E )‐nonenal: Molecular mechanism and mass spectrometric characterization of the reaction products
Author(s) -
Tatsuno Fumiya,
Lee Seon Hwa,
Oe Tomoyuki
Publication year - 2018
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.3097
Subject(s) - anserine , carnosine , chemistry , imidazole , adduct , aldehyde , histidine , schiff base , reactive intermediate , mass spectrometry , peroxide , electrospray ionization , reactive oxygen species , medicinal chemistry , stereochemistry , organic chemistry , biochemistry , chromatography , catalysis , enzyme
Imidazole dipeptides, such as carnosine (β‐alanyl‐ l ‐histidine) and anserine (β‐alanyl‐ N π ‐methyl‐ l ‐histidine), are highly localized in excitable tissues, including skeletal muscle and nervous tissue, and play important roles such as scavenging reactive oxygen species and quenching reactive aldehydes. We have demonstrated several reactions between imidazole dipeptides (namely, carnosine, and anserine) and a lipid peroxide‐derived reactive aldehyde 4‐oxo‐2( E )‐nonenal. Seven carnosine adducts and two anserine adducts were characterized using liquid chromatography/electrospray ionization‐multiple‐stage mass spectrometry. Adduct formation occurred between imidazole dipeptides and 4‐oxo‐2( E )‐nonenal mainly through Michael addition, Schiff base formation, and/or Paal‐Knorr reaction. The reactions were much more complicated than the reaction with a similar lipid peroxide‐derived reactive aldehyde, 4‐hydroxy‐2( E )‐nonenal.