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MALDI mass spectrometry‐based sequence analysis of arginine‐containing glycopeptides: improved fragmentation of glycan and peptide chains by modifying arginine residue
Author(s) -
Taniguchi Kenichi,
Kuyama Hiroki,
Kajihara Shigeki,
Tanaka Koichi
Publication year - 2013
Publication title -
journal of mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 121
eISSN - 1096-9888
pISSN - 1076-5174
DOI - 10.1002/jms.3241
Subject(s) - chemistry , glycopeptide , glycan , peptide , derivatization , residue (chemistry) , tandem mass spectrometry , arginine , mass spectrometry , chromatography , fragmentation (computing) , peptide sequence , amino acid , biochemistry , combinatorial chemistry , glycoprotein , computer science , gene , operating system , antibiotics
This paper describes an improved method for the sequence analysis of Arg‐containing glycopeptide by MALDI mass spectrometry (MS). The method uses amino group derivatization (4‐aza‐6‐(2,6‐dimethyl‐1‐piperidinyl)‐5‐oxohexanoic acid N ‐succinimidyl ester) and removal (carboxypeptidase B) or modification (peptidylarginine deiminase 4) of the arginine residue of the peptide. The derivatization attaches a basic tertiary amine moiety onto the peptides, and the enzymatic treatment removes or modifies the arginine residue. Fragmentation of the resulting glycopeptide under low‐energy collision‐induced dissociation yielded a simplified ion series of both the glycan and the peptide that can facilitate their sequencing. The feasibility of the method was studied using α 1 ‐acid glycoprotein‐derived N‐linked glycopeptides, and glycan and peptide in each glycopeptide were successfully sequenced by MALDI tandem MS (MS/MS). Copyright © 2013 John Wiley & Sons, Ltd.