Interaction between explosive and analyte layers in explosive matrix-assisted plasma desorption mass spectrometry

✍ Scribed by Kristina Håkansson; Roman A. Zubarev; Ramal V. Coorey; Victor L. Talrose; Per Håkansson

• Publisher: John Wiley and Sons
• Year: 1999
• Tongue: English
• Weight: 96 KB
• Volume: 13
• Category: Article
• ISSN: 0951-4198
• DOI: 10.1002/(sici)1097-0231(19990630)13:12<1169::aid-rcm617>3.0.co;2-y

✦ Synopsis

An HMX/insulin two-layer system was chosen as a model for further investigation of the matrix properties of explosive materials for protein analytes in plasma desorption mass spectrometry. The dependencies of the molecular ion yield and average charge state as a function of the analyte thickness were studied. An increase in the charge state of multiply protonated molecular species was confirmed as the major matrix effect, with the average charge state z at the smallest thickness studied being higher than in matrix-assisted laser desorption/ionization and closer to the value obtained in electrospray ionization under standard acidic conditions. Observed charge state distributions are significantly narrower than the corresponding Poisson distributions, which suggests that the protonation of insulin is limited in plasma desorption by the number of basic sites in the molecule, similar to electrospray ionization. Both the curve displaying total molecular ion yield and the one showing the total charge (proton) yield as a function of the insulin thickness have maxima at a thickness different from an insulin monolayer. These observations diminish the significance of a matrix/ analyte interface mechanism for the explosive matrix assistance. Instead, a mechanism related to the chemical energy release during conversion of the explosive after the ion impact is proposed. As additional mechanisms, enhanced protonation of the analyte through collisions with products of the explosive decay is considered, as well as electron scavenging by other products, which leads to a higher survival probability of positively charged protein molecular ions.