Journal of the American Society for Mass Spectrometry

, Volume 14, Issue 12, pp 1373–1386

Gas-phase dissociation pathways of multiply charged peptide clusters

  • John C. Jurchen
  • David E. Garcia
  • Evan R. Williams
Focus: Ion Activation

DOI: 10.1016/j.jasms.2003.07.003

Cite this article as:
Jurchen, J.C., Garcia, D.E. & Williams, E.R. J Am Soc Mass Spectrom (2003) 14: 1373. doi:10.1016/j.jasms.2003.07.003

Abstract

Numerous studies of cluster formation and dissociation have been conducted to determine properties of matter in the transition from the condensed phase to the gas phase using materials as diverse as atomic nuclei, noble gasses, metal clusters, and amino acids. Here, electrospray ionization is used to extend the study of cluster dissociation to peptides including leucine enkephalin with 7–19 monomer units and 2–5 protons, and somatostatin with 5 monomer units and 4 protons under conditions where its intramolecular disulfide bond is either oxidized or reduced. Evaporation of neutral monomers and charge separation by cluster fission are the competing dissociation pathways of both peptides. The dominant fission product for all leucine enkephalin clusters studied is a proton-bound dimer, presumably due to the high gas-phase stability of this species. The branching ratio of the fission and evaporation processes for leucine enkephalin clusters appears to be determined by the value of z2/n for the cluster where z is the charge and n the number of monomer units in the cluster. Clusters with low and high values of z2/n dissociate primarily by evaporation and cluster fission respectively, with a sharp transition between dissociation primarily by evaporation and primarily by fission measured at a z2/n value of ∼0.5. The dependence of the dissociation pathway of a cluster on z2/n is similar to the dissociation of atomic nuclei and multiply charged metal clusters indicating that leucine enkephalin peptide clusters exist in a state that is more disordered, and possibly fluid, rather than highly structured in the dissociative transition state. The branching ratio, but not the dissociation pathway of [somatostatin5+4H]4+ is altered by the reduction of its internal disulfide bond indicating that monomer conformational flexibility plays a role in peptide cluster dissociation.

Copyright information

© American Society for Mass Spectrometry 2003

Authors and Affiliations

  • John C. Jurchen
    • 1
  • David E. Garcia
    • 1
  • Evan R. Williams
    • 1
  1. 1.Department of ChemistryUniversity of CaliforniaBerkeleyUSA