Abstract
Based on earlier investigations forming clusters by means of laser desorption of neutrals and supersonic beam expansion followed by multi photon ionization time-of-flight mass spectrometry this study concentrates on thirteen non-aromatic tripeptides and vanillic acid. Aromatic acids are commonly used as matrix in MALDI-experiments. It is shown that the structure of the cluster from a tripeptide and vanillic acid is described by a hydrogen bond between the phenolic group of the vanillic acid and the N-terminal amino function of the tripeptide and not the carboxylic group. Using the well-defined energy input in our setup the intensity of the cluster ion and the main fragmentation product, the protonated peptide, can be linked to the proton affinity of the peptides. The observed fragmentation reactions of the protonated peptides are accompanied by extensive hydrogen rearrangements yielding a- and y-fragments. The intensities of these fragments also follow the proton affinity of the tripeptides.
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