FD and FAB mass spectra of some oligopeptides of the tryptophyllin family

Mass spectra of some natural thryptophyllins and synthetic analogues have been obtained by using field desorption and fast atom bombardment as soft ionization techniques to overcome the low volatility of these oligopeptides. Field desorption spectra generally show the molecular ion as base peak; some fragments of thermal origin are present at higher emitter heating current, thus providing additional structural information. Fast atom bombardment mass spectra show a more regular fragmentation of the peptide backbone, which allow the complete amino acid sequence to be checked. The presence of two consecutive proline residues in some of the examined molecules affects their fragmentation pattern in both field desorption and fast atom bombardment mass spectrometry giving rise to spectral features which are useful from the diagnostic point of view. The two ionization methods are compared and the advantage of the combined use of both techniques is pointed out.