Protein desolvation in UV matrix-assisted laser desorption/ionization (MALDI).

Emmanuelle Sachon (1, 2) , Gilles Clodic (1) , Thierry Blasco , Gérard Bolbach (2)

1 IFR-BI - Institut de Biologie Intégrative
2 UPMC - Université Pierre et Marie Curie - Paris 6

We describe experiments in MALDI-TOF and MALDI-TOF-TOF showing that the ejection of protein-matrix cluster ions and their partial decay in the source occur in MALDI. The use of radial beam deflection and small size detector in linear mode allows detection of ions with higher time-of-flight and kinetic energy deficit. MALDI-TOF-TOF experiments were carried out by selecting chemical noise ions at m/z higher than that of a free peptide ion. Whatever the selected m/z (up to m/z 300) the molecular peptide ion appeared as the main fragment. The production of protein-matrix clusters and their partial decay in the source was found to increase with the size of the protein (MW from 1000 to 150,000 u), although it decreases with increasing charge state. These effects were observed for different matrices (HCCA and SA) and in a large laser fluence range. Experimental results and calculation highlight that a continuous decay of protein-matrix cluster ions occurs in the source. This decay-desolvation process can account for the high-mass tailing and peak shifting as well as the strong noise/background in the mass spectra of proteins.

Domaines: Chimie organique

Emmanuelle Sachon, Gilles Clodic, Thierry Blasco, Gérard Bolbach. Protein desolvation in UV matrix-assisted laser desorption/ionization (MALDI).. Journal of The American Society for Mass Spectrometry, 2007, 18 ((10)), pp.1880-90. ⟨10.1016/j.jasms.2007.07.029⟩. ⟨hal-00689879⟩