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Influence of sequence on the fragmentation of serine‐ and threonine‐containing peptides in 252 Cf‐plasma desorption mass spectrometry
Author(s) -
LamThanh Hung,
Deprun Claude,
Le Beyec Yvon
Publication year - 1990
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.1290040202
Subject(s) - chemistry , threonine , serine , peptide , mass spectrometry , fragmentation (computing) , residue (chemistry) , chromatography , biochemistry , phosphorylation , computer science , operating system
The molecular weights of four linear synthetic peptides, fragments of a snake α‐neurotoxin, were measured by 252 Cf‐plasma desorption mass spectrometry. The fragmentation phenomenon observed at the level of serine and/or threonine residue with a concomitant ion/fragment association is reported for a group of two peptides (B and D) in contrast with the group (A and C) in spite of the high ratio of serine and threonine, namely peptide A. The propensity for specific fragmentation of peptide D seems to be correlated to the repetitive sequence, (Gly‐Ser) 2 . Finally, based on the m/z of the daughter‐ions measured, we propose an overall mechanism as an N→O acyl shift analogous to that observed for serine‐ and threonine‐ containing peptides in solution chemistry.