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A rapid isolation and identification method for blocked N‐terminal peptides by isothiocyanate‐coupled magnetic nanoparticles and MS
Author(s) -
Zhao Liyan,
Zhang Yangjun,
Wei Junying,
Cao Dong,
Liu Kehui,
Qian Xiaohong
Publication year - 2009
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.200800879
Subject(s) - isothiocyanate , peptide , chemistry , magnetic nanoparticles , nanoparticle , covalent bond , fluorescein isothiocyanate , mass spectrometry , chromatography , biochemistry , combinatorial chemistry , nanotechnology , fluorescence , materials science , organic chemistry , physics , quantum mechanics
A quick isolation and identification of N‐blocked peptides from protein digest mixtures were achieved by diisothiocyanate or isothiocyanate‐coupled magnetic nanoparticles and MS. After protein digests were guanidinated and then mixed with diisothiocyanate or isothiocyanate‐coupled magnetic nanoparticles, unmodified N‐terminal peptides were covalently bound to magnetic nanoparticles, and can be removed from the mixture under magnetic field. Therefore, N‐blocked peptides could be isolated and analyzed by MALDI or ESI MS. This new strategy was demonstrated with model peptides, proteins, and the lysates of HepG2 cells.