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

doi:10.1021/ja100243h

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 journal › Article › peer-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 PrP^Sc. While PrP^Sc is known to be exceptionally stable and resistant to protease degradation, PrP^C 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 PrP^C 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 language	English
Pages (from-to)	8816-8818
Number of pages	3
Journal	Journal of the American Chemical Society
Volume	132
Issue number	26
DOIs	https://doi.org/10.1021/ja100243h
Publication status	Published - 7 Jul 2010

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title = "Conformational stability of syrian hamster prion protein PrP(90-231)",

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).",

author = "Megan Grabenauer and Thomas Wyttenbach and Narinder Sanghera and Slade, {Susan E.} and Pinheiro, {Teresa J T} and James Scrivens and Bowers, {Michael T.}",

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T1 - Conformational stability of syrian hamster prion protein PrP(90-231)

AU - Grabenauer, Megan

AU - Wyttenbach, Thomas

AU - Sanghera, Narinder

AU - Slade, Susan E.

AU - Pinheiro, Teresa J T

AU - Scrivens, James

AU - Bowers, Michael T.

PY - 2010/7/7

Y1 - 2010/7/7

N2 - 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).

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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JO - Journal of the American Chemical Society

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

Abstract

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