Mass spectrometric and chemical stability of the Asp‐Pro bond in herpes simplex virus epitope peptides compared with X‐Pro bonds of related sequences

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Abstract
The mass spectrometric analysis of the immunodominant epitope region (273–284) of herpes simplex virus type 1 (HSV‐1) glycoprotein D (gD) showed a favoured fission at the Asp‐Pro peptide bond. The fast atom bombardment collision induced dissociation (FAB‐CID) study of closely related X‐Pro peptides documented that neither the length nor the amino acid composition of the peptide has a significant influence on this preferential cleavage. At the same time the DP bond proved to be sensitive to acidic conditions in the course of peptide synthesis. These observations prompted us to compare the chemical and mass spectrometric stability of a new set of nonapeptides related to the 273–284 epitope region of gD, i.e. SALLEDPVG and SALLEXPVG peptides, where X = A, K, I, S, F, E or D, respectively. The chemical stability of these peptides during acidic hydrolysis was investigated by electrospray ionization mass spectrometry (ESI‐MS) and the products were identified by ESI‐MS and on‐line high performance liquid chromatography—mass spectrometry (HPLC‐MS). The mass spectrometric fragmentation and bond stability of the untreated peptide samples were also studied using ESI‐MS and liquid secondary ion mass spectrometry (LSIMS). Both the chemical hydrolysis and the mass spectrometric fragmentation showed that the Asp‐Pro bond could easily be cleaved, while the KP bond proved to be stable under both circumstances. On the other hand, the XP bond (X = A, I, S, F or E) fragmented easily under the mass spectrometric conditions, but was not sensitive to the acidolysis. Copyright © 2002 European Peptide Society and John Wiley & Sons, Ltd.
Funding Information
  • Hungarian Scientific Research Foundation (T 019306; T 030838.)
  • Hungarian Ministry of Culture (0101/1997.)
  • EU-Network (ERB4050PL932014.)