Complete and selective nitration of tyrosine residue in peptides caused by ultraviolet matrix-assisted laser desorption/ionization.

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. NO attack reaction mechanism by Long et al. and the C-NO 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).