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The conventional MALDI\u2010ISD is initiated by the hydrogen transfer from reducing matrix molecules to peptide backbone, leading to <jats:italic>c<\/jats:italic>\u2032\u2010 and <jats:italic>z<\/jats:italic>\u2032\u2010series ions. In contrast, when an oxidizing chemical 5\u2010nitrosalicylic acid (5\u2010NSA) is served as the MALDI\u2010ISD matrix, <jats:italic>a<\/jats:italic>\u2010 and <jats:italic>x<\/jats:italic>\u2010series ions are specifically generated by hydrogen abstraction from peptide backbone to matrix molecule. The 5\u2010NSA provides useful complementary information to the conventional MALDI\u2010ISD for the analysis of amino acid sequencing and site localization of phosphorylation in peptides. The MALDI\u2010ISD with reducing and oxidizing matrix could be a useful method for the <jats:italic>de novo<\/jats:italic> peptide sequencing. 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