Performances and limits of plasma desorption mass spectrometry in the primary structure determination of proteins.

The resolution, sensitivity, matrix effect, cationization and spectral suppression in plasma desorption mass spectrometry (PD-MS) were investigated in the context of peptide analysis. Excessive cationization may be avoided by the addition of citric acid on the target. The importance of the relative net charge of peptides in PD-MS spectra suppression was confirmed. Esterification of peptides is shown to be an easy way to overcome spectral suppression. Provided that cationization and spectral suppression of peptides are under control, PD-MS is an excellent tool for protein sequence analysis, affording the necessary complement to automated Edman degradation.