Estimation of nucleoside proton affinity scale from dissociations of hydrogen-bound heterodimer constituted with amino acid partners

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Eur. J. Mass Spectrom. 6, 451 - 455 (2000)

Estimation of nucleoside proton affinity scale from dissociations of hydrogen-bound heterodimer constituted with amino acid partners

S. Alves, F. Fournier and J.-C. Tabet^*
Laboratoire de Chimle Structurale Organique et Biologique, UMR 7613, Université Pierre et Marie Curie, Paris Cedex 05, France
M. Quelquejeu and J.M. Valery
Laboratoire des Glucides, UMR 7613, Université Pierre et Marie Curie, Paris Cedex 05, France

ABSTRACT:

Nucleoside proton affinity was determined using Cooks kinetic method. An ion trap mass spectrometer coupled with an external electrospray source was used to form proton-bound homo- and heterodimers from modified uridines and amino acids at low effective temperature. The experimental proton affinity (PA) values obtained show the effects of structural changes in nucleosides on PA values (i.e. U < dU and 5IdU < dU < dT). The calculated values are consistent with those reported by tandem sector instruments. In this way, an hypothesis on the interaction site of the heterodimers is proposed: the amino groups are likely to interact with the proton (in the dimer) as expected from its solution behavior.

Keywords: ESI, ion trap mass spectrometer, nucleoside proton affinities, Cooks kinetic method

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