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Updated: Aug 22, 2025

Nitropeptide Profiling and Identification Illustrated by Angiotensin II
Published on: June 16, 2019
Complete and selective nitration of tyrosine residue in peptides caused by ultraviolet matrix-assisted laser
1Graduate School in Nanobioscience, Yokohama City University, 22-2 Seto, Kanazawa-ku, Yokohama, 236-0027m, Japan. takayama@yokohama-cu.ac.jp.
Abstract:
Complete and highly selective nitration of tyrosine (Tyr) as a residue-specific modification in peptides was found without side reactions, using ultraviolet matrix-assisted laser desorption/ionization (UV-MALDI) with a nitroaromatic reagent 3, 5-dinitrosalicylic acid (3,5-DNSA). The tyrosine nitration supported two propositions, namely, the UV-induced. NO2 attack reaction mechanism by Long et al. and the C-NO2 homolysis as a thermal process by Wiik et al. and Furman et al. With the UV-MALDI of peptides, a residue-specific reaction was observed in glycine (Gly) residue, i.e., an oxidation of the alpha-carbon of Gly due to attack of hydroxyl radical (.OH).
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