Conformational stability of syrian hamster prion protein PrP(90-231)

Megan Grabenauer, Thomas Wyttenbach, Narinder Sanghera, Susan E. Slade, Teresa J T Pinheiro, James Scrivens, Michael T. Bowers

Research output: Contribution to journalArticleResearchpeer-review

24 Citations (Scopus)

Abstract

Many transmissible spongiform encephalopathies (TSEs) are believed to be caused by a misfolded form of the normal cellular prion protein (PrP C) known as PrPSc. While PrPSc is known to be exceptionally stable and resistant to protease degradation, PrPC has not shown these same unusual characteristics. However, using ion mobility spectrometry mass spectrometry (IMS-MS), we found evidence for at least one very stable conformation of a truncated form of recombinant PrPC consisting of residues 90-231, which resists unfolding in the absence of solvent at high injection energies and at temperatures in excess of 600 K. We also report the first absolute collision cross sections measured for recombinant Syrian hamster prion protein PrP(90-231).

Original languageEnglish
Pages (from-to)8816-8818
Number of pages3
JournalJournal of the American Chemical Society
Volume132
Issue number26
DOIs
Publication statusPublished - 7 Jul 2010

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Prion Diseases
Mesocricetus
Protein C
Mass Spectrometry
Spectrum Analysis
Peptide Hydrolases
Ions
Injections
Temperature
Spectrometry
Mass spectrometry
Conformations
Degradation
prion protein (90-231)
Prion Proteins
Prions

Cite this

Grabenauer, M., Wyttenbach, T., Sanghera, N., Slade, S. E., Pinheiro, T. J. T., Scrivens, J., & Bowers, M. T. (2010). Conformational stability of syrian hamster prion protein PrP(90-231). Journal of the American Chemical Society, 132(26), 8816-8818. https://doi.org/10.1021/ja100243h
Grabenauer, Megan ; Wyttenbach, Thomas ; Sanghera, Narinder ; Slade, Susan E. ; Pinheiro, Teresa J T ; Scrivens, James ; Bowers, Michael T. / Conformational stability of syrian hamster prion protein PrP(90-231). In: Journal of the American Chemical Society. 2010 ; Vol. 132, No. 26. pp. 8816-8818.
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abstract = "Many transmissible spongiform encephalopathies (TSEs) are believed to be caused by a misfolded form of the normal cellular prion protein (PrP C) known as PrPSc. While PrPSc is known to be exceptionally stable and resistant to protease degradation, PrPC has not shown these same unusual characteristics. However, using ion mobility spectrometry mass spectrometry (IMS-MS), we found evidence for at least one very stable conformation of a truncated form of recombinant PrPC consisting of residues 90-231, which resists unfolding in the absence of solvent at high injection energies and at temperatures in excess of 600 K. We also report the first absolute collision cross sections measured for recombinant Syrian hamster prion protein PrP(90-231).",
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Grabenauer, M, Wyttenbach, T, Sanghera, N, Slade, SE, Pinheiro, TJT, Scrivens, J & Bowers, MT 2010, 'Conformational stability of syrian hamster prion protein PrP(90-231)', Journal of the American Chemical Society, vol. 132, no. 26, pp. 8816-8818. https://doi.org/10.1021/ja100243h

Conformational stability of syrian hamster prion protein PrP(90-231). / Grabenauer, Megan; Wyttenbach, Thomas; Sanghera, Narinder; Slade, Susan E.; Pinheiro, Teresa J T; Scrivens, James ; Bowers, Michael T.

In: Journal of the American Chemical Society, Vol. 132, No. 26, 07.07.2010, p. 8816-8818.

Research output: Contribution to journalArticleResearchpeer-review

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AU - Scrivens, James

AU - Bowers, Michael T.

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AB - Many transmissible spongiform encephalopathies (TSEs) are believed to be caused by a misfolded form of the normal cellular prion protein (PrP C) known as PrPSc. While PrPSc is known to be exceptionally stable and resistant to protease degradation, PrPC has not shown these same unusual characteristics. However, using ion mobility spectrometry mass spectrometry (IMS-MS), we found evidence for at least one very stable conformation of a truncated form of recombinant PrPC consisting of residues 90-231, which resists unfolding in the absence of solvent at high injection energies and at temperatures in excess of 600 K. We also report the first absolute collision cross sections measured for recombinant Syrian hamster prion protein PrP(90-231).

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Grabenauer M, Wyttenbach T, Sanghera N, Slade SE, Pinheiro TJT, Scrivens J et al. Conformational stability of syrian hamster prion protein PrP(90-231). Journal of the American Chemical Society. 2010 Jul 7;132(26):8816-8818. https://doi.org/10.1021/ja100243h