Journal of Chemical Physics 2011-02-07

Bond dissociation of the dipeptide dialanine and its derivative alanine anhydride induced by low energy electrons.

Elahe Alizadeh, David Gschliesser, Peter Bartl, Michaela Hager, Achim Edtbauer, Violaine Vizcaino, Andreas Mauracher, Michael Probst, Tilmann D Märk, Sylwia Ptasińska, Nigel J Mason, Stephan Denifl, Paul Scheier

Index: J. Chem. Phys. 134(5) , 054305, (2011)

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Abstract

Dissociative electron attachment to dialanine and alanine anhydride has been studied in the gas phase utilizing a double focusing two sector field mass spectrometer. We show that low-energy electrons (i.e., electrons with kinetic energies from near zero up to 13 eV) attach to these molecules and subsequently dissociate to form a number of anionic fragments. Anion efficiency curves are recorded for the most abundant anions by measuring the ion yield as a function of the incident electron energy. The present experiments show that as for single amino acids (M), e.g., glycine, alanine, valine, and proline, the dehydrogenated closed shell anion (M-H)(-) is the most dominant reaction product. The interpretation of the experiments is aided by quantum chemical calculations based on density functional theory, by which the electrostatic potential and molecular orbitals are calculated and the initial electron attachment process prior to dissociation is investigated.