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The sodium ion affinity of glycylglycine

Abstract : The sodium ion affinity of the simplest peptide, glycylglycine (GlyGly), is determined by the kinetic method, from the dissociation kinetics of Na+-bound dimers of GlyGly and amino acid reference bases. The dimer ions are formed by electrospray ionization and their competitive dissociations to the metalated monomers are probed by collisionally activated dissociation in a quadrupole ion trap mass spectrometer. The experimental value derived is 203±8 kJ mol-1 (ΔHNa at 298 K). Concurrent high-level ab initio calculations predict a GlyGly-Na+ bond enthalpy of 200 kJ mol-1, in excellent agreement with the experimental result. The most stable structure of the GlyGly-Na+ complex found by the ab initio calculations involves solvation of the metal charge by the multidentate GlyGly ligand. The Na+ affinity reported here lies substantially above older literature values (177-181 kJ mol-1). Plausible reasons for the earlier underestimations are briefly discussed.
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Contributor : Denis Roura Connect in order to contact the contributor
Submitted on : Thursday, December 12, 2013 - 8:08:38 PM
Last modification on : Wednesday, December 15, 2021 - 10:00:38 AM

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M.M. Kish, C. Wesdemiotis, Gilles Ohanessian. The sodium ion affinity of glycylglycine. Journal of Physical Chemistry B, 2004, 108 (9), pp.3086-3091. ⟨10.1021/jp0367676⟩. ⟨hal-00917366⟩



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