Journal of the American Society for Mass Spectrometry

, Volume 17, Issue 12, pp 1712–1716

Generation and detection of multiply-charged peptides and proteins by matrix-assisted laser desorption electrospray ionization (MALDESI) fourier transform ion cyclotron resonance mass spectrometry

  • Jason S. Sampson
  • Adam M. Hawkridge
  • David C. Muddiman
Short Communication

DOI: 10.1016/j.jasms.2006.08.003

Cite this article as:
Sampson, J.S., Hawkridge, A.M. & Muddiman, D.C. J Am Soc Mass Spectrom (2006) 17: 1712. doi:10.1016/j.jasms.2006.08.003

Abstract

We report the coupling of a hybrid ionization source, matrix-assisted laser desorption electrospray ionization (MALDESI), to a Fourier transform-ion cyclotron resonance mass spectrometer (FT-ICR MS). The details of the source design and initial data are presented. Analysis of peptides and proteins ranging from 1 to 8.6 kDa resulted in high resolving power single-acquisition FT-ICR mass spectra with average charge-states highly correlated to those obtained by nanoESI, thus, providing strong evidence that the ESI process dictates the observed charge-state distribution. Importantly, unlike the recently introduced electrospray assisted laser desorption ionization (ELDI) source reported by Shiea and coworkers [1, 2], the data we have obtained to date rely on the use of an organic acid matrix. The results presented herein provide insight into the charging mechanism of this emerging ionization approach, while also expanding the utility of FT-ICR MS for top-down protein and complex mixture analysis.

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Copyright information

© American Society for Mass Spectrometry 2006

Authors and Affiliations

  • Jason S. Sampson
    • 1
  • Adam M. Hawkridge
    • 1
  • David C. Muddiman
    • 1
  1. 1.W. M. Keck FT-ICR Mass Spectrometry Laboratory, Department of ChemistryNorth Carolina State UniversityRaleighUSA