Stability of Asp-Pro bond under high and low energy collision induced dissociation conditions in the immunodominant epitope region of herpes simplex virion glycoprotein D.
A series of truncated Herpes simplex virion peptides studied by fast atom bombardment mass spectrometry under high and low energy collision induced dissociation conditions showed preferential fragmentation of the aspartyl-proline amide bond, compared to other peptide bonds. Electrospray ionization investigation proved that this favoured fragmentation can not be attributed to only the known proline effect, as a change from Asp to Asn in the peptide yielded an Asn-Pro bond which was found to be stable under the same ionization conditions. This mass spectrometric behaviour is in good agreement with the observation that DP bonds are sensitive to acidic conditions.
Central Research Institute for Chemistry of the Hungarian Academy of Sciences, Budapest, Hungary.
M
M
Mák
G
G
Mezö
Z
Z
Skribanek
F
F
Hudecz
D000595:Amino Acid Sequence; D004151:Dipeptides / Q000032:analysis / Q000737:chemistry*; D000939:Epitopes / Q000032:analysis / Q000737:chemistry*; D008401:Gas Chromatography-Mass Spectrometry; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000032:analysis / Q000737:chemistry; D014759:Viral Envelope Proteins / Q000032:analysis / Q000737:chemistry*
D004151:Dipeptides; D000939:Epitopes; D009842:Oligopeptides; D014759:Viral Envelope Proteins; C039447:glycoprotein D, Human herpesvirus 1; C070752:aspartyl-proline