In-source fragmentation of peptide aldehydes and acetals: influence of peptide length and charge state.
The use of in-source collision-induced dissociation (CID) was evaluated to generate structural information on peptide aldehydes, which represent an important class of compounds as inhibitors for serine and cysteine proteases and as key intermediates for protein engineering. By studying five peptide aldehydes of different lengths, and their peptide acetal counterparts, mass to charge (m/z) dependency of in-source fragmentation was established for peptides that differ only by their C-terminal functionalization. In-source fragmentation of peptide aldehydes and acetals leads to the same final ion, probably via a similar mechanism. Moreover, the gas-phase information obtained here reflects the equilibrium occurring in solution between the peptide aldehyde and its hydrated form, which was retained during the ionization process. The equilibrium constant was determined to be close to unity. Disturbance of this equilibrium should enable the stability of covalent hydration of a given series of aldehydes to be compared.
Buré
C
C
Centre de Biophysique Moléculaire, CNRS UPR 4301, rue Charles Sadron, 45071 Orléans Cedex 02, France. bure@cnrs-orleans.fr
Gobert
W
W
Lelièvre
D
D
Delmas
A
A
D000447:Aldehydes / Q000737:chemistry*; D000595:Amino Acid Sequence; D004563:Electrochemistry; D008401:Gas Chromatography-Mass Spectrometry; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry*; D015842:Serine Proteinase Inhibitors / Q000737:chemistry*; D021241:Spectrometry, Mass, Electrospray Ionization
D000447:Aldehydes; D010455:Peptides; D015842:Serine Proteinase Inhibitors