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A new deuterated alkylating agent for quantitative proteomics
Author(s) -
Sebastiano Roberto,
Citterio Attilio,
Lapadula Marta,
Righetti Pier Giorgio
Publication year - 2003
Publication title -
rapid communications in mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.528
H-Index - 136
eISSN - 1097-0231
pISSN - 0951-4198
DOI - 10.1002/rcm.1206
Subject(s) - chemistry , iodoacetamide , alkylation , proteomics , deuterium , acrylamide , molecule , proteome , double bond , combinatorial chemistry , cysteine , biochemistry , organic chemistry , enzyme , physics , polymer , quantum mechanics , copolymer , gene , catalysis
Weakly basic molecules containing a double bond, such as 2‐ and 4‐vinylpyridine, are able to react and selectively alkylate –SH groups in proteins, thus preventing their re‐oxidation to disulphide bridges. In contrast to conventional alkylating agents such as iodoacetamide and non‐charged acrylamide derivatives, such molecules achieve 100% alkylation of all –SH residues, even in complex proteins, without reacting with other functional groups. Their use is particularly effective in proteome analysis and more generally for analyzing proteins in which the –SH groups should be blocked. Additionally, the use of vinylpyridines, partially or totally deuterated and thus with a mass difference compared with their non‐deuterated counterparts of 4–7 Da, allows studies of induction/repression of protein synthesis (quantitative proteomics). Copyright © 2003 John Wiley & Sons, Ltd.