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Improving mass spectrometric sequencing of arginine‐containing peptides by derivatization with acetylacetone
Author(s) -
Dikler Sergei,
Kelly Jeffery W.,
Russell David H.
Publication year - 1997
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/(sici)1096-9888(199712)32:12<1337::aid-jms599>3.0.co;2-x
Subject(s) - chemistry , mass spectrometry , peptide , matrix assisted laser desorption/ionization , derivatization , arginine , chromatography , fragmentation (computing) , reflectron , protein primary structure , peptide sequence , ion , amino acid , desorption , biochemistry , organic chemistry , ionization , time of flight mass spectrometry , adsorption , computer science , operating system , gene
Modification of arginine residues in bradykinin, [1–5]‐bradykinin, splenopentin and two synthetic pentapeptides with acetylacetone (pentane‐2,4‐dione) significantly increases the relative abundance of sequence‐specific fragment ions produced by matrix‐assisted laser desorption/ionization (MALDI). The fragmentation efficiency as measured by post‐source decay in a reflectron time‐of‐flight mass spectrometer increases by a factor of 2–3.5. Peptide bonds adjacent to modified residues are more susceptible to cleavage than in the non‐derivatized peptide ions. The increased lability of these bonds gives rise to more complete sequence information. In addition, the relative abundances of sequence‐specific fragment ions are enhanced. This strategy makes it possible to obtain valuable structural information from arginine‐containing peptides that otherwise do not fragment well. © 1997 John Wiley & Sons, Ltd.