An infrared spectroscopy approach to follow β-sheet formation in peptide amyloid assemblies
SCIE
SCOPUS
- Title
- An infrared spectroscopy approach to follow β-sheet formation in peptide amyloid assemblies
- Authors
- SEO, JONGCHEOL; HOFFMANN, WALDEMAR; WARNKE, STEPHAN; HUANG, XING; GEWINNER, SANDY; SCHÖLLKOPF, WIELAND; BOWERS, MICHAEL T.; VON HELDEN, GERT; PAGEL, KEVIN
- Date Issued
- 2017-02
- Publisher
- NATURE PUBLISHING GROUP
- 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 beta-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 beta-sheet. In addition, our data show that the more-extended variants of each oligomer generally exhibit increased beta-sheet content.
- URI
- https://oasis.postech.ac.kr/handle/2014.oak/94534
- DOI
- 10.1038/nchem.2615
- ISSN
- 1755-4330
- Article Type
- Article
- Citation
- Nature Chemistry, vol. 9, no. 1, page. 39 - 44, 2017-02
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