Analytical laser induced liquid beam desorption mass spectrometry of protonated amino acids and their non-covalently bound aggregates
MPI für Biophysikalische Chemie, Am Faßberg 11, 37077 Göttingen, Germany
2 MPI für Strömungsforschung, Bunsenstraße 10, 37073 Göttingen, Germany
Corresponding author: a email@example.com
Published online: 13 September 2002
We have used analytical laser induced liquid beam desorption in combination with high resolution mass spectrometry () for the study of protonated amino acids (ornithine, citrulline, lysine, arginine) and their non-covalently bound complexes in the gas phase desorbed from water solutions. We report studies in which the desorption mechanism has been investigated. The results imply that biomolecule desorption at our conditions is a single step process involving laser heating of the solvent above its supercritical temperature, a rapid expansion, ion recombination and finally isolation and desorption of only a small fraction of preformed ions and charged aggregates. In addition, we report an investigation of the aqueous solution concentration and pH-dependence of the laser induced desorption of protonated species (monomers and dimers). The experimental findings suggest that the desorption process depends critically upon the proton affinity of the molecules, the concentration of other ions, and of the pH value of the solution. Therefore the ion concentrations measured in the gas phase very likely reflect solution properties (equilibrium concentrations). Arginine self-assembles large non-covalent singly protonated multimers (n=1...8) when sampled by IR laser induced water beam desorption mass spectrometry. The structures of these aggregates may resemble those of the solid state and may be preformed in solution prior to desorption. A desorption of mixtures of amino acids in water solution enabled us to study (mixed) protonated dimers, one of the various applications of the present technique. Reasons for preferred dimerization – leading to simple cases of molecular recognition – as well as less preferred binding is discussed in terms of the number of specific H-bonds that can be established in the clusters.
PACS: 82.80.Rt – Time of flight mass spectrometry / 87.15.-v – Biomolecules: structure and physical properties / 87.15.Nn – Properties of solutions; aggregation and crystallization of macromolecules
© EDP Sciences, Società Italiana di Fisica, Springer-Verlag, 2002