Open AccessQuantification of Tryptic Peptides in Quadrupole Ion Trap Using High-Mass Signals Derived from Isotope-Coded N-Acetyl Dipeptide Tags
Author(s) -
Jongcheol Seo,
Hye–Joo Yoon,
Seung Koo Shin
Publication year - 2011
Publication title -
journal of the american society for mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.961
H-Index - 127
eISSN - 1879-1123
pISSN - 1044-0305
DOI - 10.1007/s13361-011-0189-6
Subject(s) - chemistry , isobaric labeling , dipeptide , mass spectrometry , tandem mass spectrometry , tandem mass tag , quadrupole ion trap , peptide , chromatography , protein mass spectrometry , isobaric process , ion trap , isotope , sample preparation in mass spectrometry , cleavage (geology) , quadrupole , top down proteomics , quantitative proteomics , proteomics , biochemistry , electrospray ionization , fracture (geology) , engineering , quantum mechanics , thermodynamics , physics , geotechnical engineering , atomic physics , gene
Isotope-labeled N-acetyl dipeptides (Ac-Xxx-Ala) are coupled to the primary amines of tryptic peptides and then analyzed by tandem mass spectrometry. Amide bond cleavage between Xxx and Ala provides both low- and high-mass isotope-coded signals for quantification of peptides. Especially, facile cleavage at the modified lysine side chain yields very strong high-mass quantitation signals in a noise-free region. Tagging tryptic peptides with isobaric N-acetyl dipeptides is a viable strategy for accurate quantification of proteins, which can be used with most quadrupole ion trap mass spectrometers carrying the 1/3 mass cut-off problem.