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  An infrared spectroscopy approach to follow β-sheet formation in peptide amyloid assemblies

Seo, J., Hoffmann, W., Warnke, S., Huang, X., Gewinner, S., Schöllkopf, W., et al. (2017). An infrared spectroscopy approach to follow β-sheet formation in peptide amyloid assemblies. Nature Chemistry, 9(1), 39-44. doi:10.1038/nchem.2615.

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Seo, Jongcheol1, Author              
Hoffmann, Waldemar1, 2, Author              
Warnke, Stephan1, Author              
Huang, Xing3, Author              
Gewinner, Sandy1, Author              
Schöllkopf, Wieland1, Author              
Bowers, Michael T.4, Author
Helden, Gert von1, Author              
Pagel, Kevin1, 2, Author              
Affiliations:
1Molecular Physics, Fritz Haber Institute, Max Planck Society, ou_634545              
2Institute of Chemistry and Biochemistry, Freie Universität Berlin, Takustrasse 3, Berlin 14195, Germany, ou_persistent22              
3Inorganic Chemistry, Fritz Haber Institute, Max Planck Society, ou_24023              
4Department of Chemistry and Biochemistry, University of California Santa Barbara, Santa Barbara, California 93106, USA, ou_persistent22              

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 Abstract: Amyloidogenic peptides and proteins play a crucial role in a variety of neurodegenerative disorders such as Alzheimer's and Parkinson's disease. These proteins undergo a spontaneous transition from a soluble, often partially folded form, into insoluble amyloid fibrils that are rich in β-sheets. Increasing evidence suggests that highly dynamic, polydisperse folding intermediates, which occur during fibril formation, are the toxic species in the amyloid-related diseases. Traditional condensed-phase methods are of limited use for characterizing these states because they typically only provide ensemble averages rather than information about individual oligomers. Here we report the first direct secondary-structure analysis of individual amyloid intermediates using a combination of ion mobility spectrometry–mass spectrometry and gas-phase infrared spectroscopy. Our data reveal that oligomers of the fibril-forming peptide segments VEALYL and YVEALL, which consist of 4–9 peptide strands, can contain a significant amount of β-sheet. In addition, our data show that the more-extended variants of each oligomer generally exhibit increased β-sheet content.

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 Dates: 2015-11-262016-08-102016-09-262017-01
 Publication Status: Published in print
 Pages: 6
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1038/nchem.2615
 Degree: -

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Title: Nature Chemistry
  Abbreviation : Nat. Chem.
Source Genre: Journal
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Publ. Info: London, UK : Nature Publishing Group
Pages: 6 Volume / Issue: 9 (1) Sequence Number: - Start / End Page: 39 - 44 Identifier: ISSN: 1755-4330
CoNE: https://pure.mpg.de/cone/journals/resource/1755-4330