ArticleFrontiers in bioengineering and biotechnology2021
SAXS/WAXS Investigation of Amyloid-β(16-22) Peptide Nanotubes.
Article in Frontiers in bioengineering and biotechnology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
What it found
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Who cites it
5 citing papers in PubMed.
- Small-angle scattering studies on diverse peptide-based nanotube and helical ribbon structures reveal distinct form and structure factors.Journal of applied crystallography · 2025Article
- Current and future perspectives for structural biology at the Grenoble EPN campus: a comprehensive overview.Journal of synchrotron radiation · 2025Review
- Amyloid β 42 fibril structure based on small-angle scattering.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Deterministic chaos in the self-assembly of β sheet nanotubes from an amphipathic oligopeptide.Matter · 2021Article
- Multiscale Structural Elucidation of Peptide Nanotubes by X-Ray Scattering Methods.Frontiers in bioengineering and biotechnology · 2021Review
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
This brief report presents an X-ray scattering investigation of self-assembled nanotubes formed by a short peptide. X-ray scattering methods enable multiscale structural elucidation of these nanotubes in solution under the same conditions involved in the self-assembly process. In particular, the dimensions of nanotubes and the crystalline organization within their walls can be determined quantitatively. This is illustrated in the case of amyloid-β(16-22) peptide nanotubes.
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Registered trials
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