Influence of sequence on the fragmentation of serine- and threonine-containing peptides in 252Cf-plasma desorption mass spectrometry.
The molecular weights of four linear synthetic peptides, fragments of a snake alpha-neurotoxin, were measured by 252Cf-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.
Lam-Thanh
H
H
Service de Biochimie, CEN, Saclay, Gif-sur-Yvette, France.
Deprun
C
C
Le Beyec
Y
Y
D000595:Amino Acid Sequence; D000818:Animals; D003039:Cobra Neurotoxin Proteins; D066298:In Vitro Techniques; D013058:Mass Spectrometry / Q000379:methods; D008969:Molecular Sequence Data; D010446:Peptide Fragments
D003039:Cobra Neurotoxin Proteins; D010446:Peptide Fragments