Abstract
Matrix-assisted laser desorption ionization ion mobility coupled to orthogonal time-of-flight mass spectrometry (MALDI-IM-oTOF MS) is evaluated as a tool for studying non-covalent complex (NCX) formation between peptides. The NCX formed between dynorphin 1–7 and Mini Gastrin I is used as a model system for comparison to previous MALDI experiments (Woods, A. S.; Huestis, M. A. J. Am. Soc. Mass Spectrom. 2001, 12, 88–96). The dynorphin 1–7/Mini Gastrin I complex is stable after more than a ms drift time through the He filled mobility cell. Furthermore, the effects of solution pH on NCX ion signal intensity is measured both by MALDI-IM-MS analysis and by nanoelectrospray mass spectrometry. When compared to the previous MALDI study this work shows that all three techniques give similar results. In addition, fragmentation can be observed from of the non-covalent complex parent ion that occurs prior to TOF mass analysis but after mobility separation, thus providing NCX composition information.
Article PDF
Avoid common mistakes on your manuscript.
References
Loo, J. A. Mass Spectrom. Rev. 1997, 16, 1–17.
Farmer, T. B.; Caprioli, R. M. J. Mass Spectrom. 1998, 33, 697–704.
Woods, A. S.; Huestis, M. A. J. Am. Soc. Mass Spectrom. 2001, 12, 88–96.
Kyte, J. Structure in Protein Chemistry. Garland Publishing, Inc.: New York, 1995 Chap II.
Creighton, T. E. Proteins Structure and Molecular Properties; 2nd ed. W. H. Freeman and Company: New York, 1993, Chap I.
Woods, A. S.; Buchsbaum, J. C.; Worrall, T. A.; Cotter, R. J. Berg, J. M. Anal. Chem. 1995, 67, 4462–4465.
Lin, S.; Cotter, R. J.; Woods, A. S. Proteins: Structure, Function and Genetics 1998, 2, 12–21.
Lin, S.; Long, S.; Ramirez, S. M.; Cotter, R. J.; Woods, A. S. Anal. Chem. 2000, 72, 2635–2640.
Anfinsen, C. B. Science 1973, 181, 223–230.
Gillig, K. J.; Ruotolo, B. T.; Stone, E. G.; Russell, D. H.; Fuhrer, K.; Gonin, M.; Schultz, J. A. Anal. Chem. 2000, 72, 3965–3971.
McDaniel, E. W.; Mason, E. A. The Mobility and Diffusion of Ions in Gases. Wiley: New York, 1973; 31–93.
Mason, E. A. Plasma Chromatography. Carr, T. W., Ed., Plenum Press: New York, 1984; 80–83.
Wyttenbach, T.; vonHelden, G.; Bowers, M. T. J. Am. Chem. Soc. 1996, 118, 8355–8364.
Counterman, A. E.; Clemmer, D. E. J. Am. Chem. Soc. 1999, 121, 4031–4039.
Wu, C.; Siems, W. F.; Asbury, G. R.; Hill, H. H., Jr. Anal. Chem. 1998, 70, 4929–4938.
Wu, C.; Siems, W. F.; Klasmeier, J.; Hill, H. H. Anal. Chem. 2000, 72, 391–395.
Kinnear, B. S.; Hartings, M. R.; Jarrold, M. F. J. Am. Chem. Soc. 2001, 123, 5660–5667.
Gidden, J.; Bushnell, J. E.; Bowers, M. T. J. Am. Chem. Soc. 2001, 123, 5610–5611.
Srebalus, C. A.; Li, J.; Marshall, W. S.; Clemmer, D. E. Anal. Chem. 1999, 71, 3198–3927.
Jarrold, M. F. Annu. Rev. Phys. Chem. 2000, 51, 179–207.
Ruotolo, B. T.; Gillig, K. J.; Stone, E. G.; Russell, D. H.; Fuhrer, K.; Schultz, J. A. Int. J. Mass Spectrom. to be published.
Gillig, K. J.; Russell, D. H. International application published under the Patent Cooperation Treaty WO 01/65589 A1.
Author information
Authors and Affiliations
Corresponding author
Rights and permissions
About this article
Cite this article
Woods, A.S., Koomen, J.M., Ruotolo, B.T. et al. A study of peptide—Peptide interactions using MALDI ion mobility o-TOF and ESI mass spectrometry. J Am Soc Mass Spectrom 13, 166–169 (2002). https://doi.org/10.1016/S1044-0305(01)00348-8
Received:
Revised:
Accepted:
Issue Date:
DOI: https://doi.org/10.1016/S1044-0305(01)00348-8