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| Verfasst von: | Taş, Karin [VerfasserIn]  |
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| | Volta, Beatrice Dalla [VerfasserIn] |
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| | Lindner, Christina [VerfasserIn] |
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| | El Bounkari, Omar [VerfasserIn] |
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| | Hille, Kathleen [VerfasserIn] |
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| | Tian, Yuan [VerfasserIn] |
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| | Puig-Bosch, Xènia [VerfasserIn] |
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| | Ballmann, Markus [VerfasserIn] |
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| | Hornung, Simon [VerfasserIn] |
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| | Ortner, Martin [VerfasserIn] |
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| | Prem, Sophia [VerfasserIn] |
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| | Meier, Laura [VerfasserIn] |
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| | Rammes, Gerhard [VerfasserIn] |
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| | Haslbeck, Martin [VerfasserIn] |
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| | Weber, Christian [VerfasserIn] |
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| | Megens, Remco T. A. [VerfasserIn] |
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| | Bernhagen, Jürgen [VerfasserIn] |
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| | Kapurniotu, Aphrodite [VerfasserIn] |
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| Titel: | Designed peptides as nanomolar cross-amyloid inhibitors acting via supramolecular nanofiber co-assembly |
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| Verf.angabe: | Karin Taş, Beatrice Dalla Volta, Christina Lindner, Omar El Bounkari, Kathleen Hille, Yuan Tian, Xènia Puig-Bosch, Markus Ballmann, Simon Hornung, Martin Ortner, Sophia Prem, Laura Meier, Gerhard Rammes, Martin Haslbeck, Christian Weber, Remco T.A. Megens, Jürgen Bernhagen & Aphrodite Kapurniotu |
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| E-Jahr: | 2022 |
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| Jahr: | 25 August 2022 |
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| Umfang: | 22 S. |
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| Fussnoten: | Gesehen am 20.12.2022 |
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| Titel Quelle: | Enthalten in: Nature Communications |
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| Ort Quelle: | [London] : Nature Publishing Group UK, 2010 |
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| Jahr Quelle: | 2022 |
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| Band/Heft Quelle: | 13(2022), Artikel-ID 5004, Seite 1-22 |
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| ISSN Quelle: | 2041-1723 |
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| Abstract: | Amyloid self-assembly is linked to numerous devastating cell-degenerative diseases. However, designing inhibitors of this pathogenic process remains a major challenge. Cross-interactions between amyloid-β peptide (Aβ) and islet amyloid polypeptide (IAPP), key polypeptides of Alzheimer’s disease (AD) and type 2 diabetes (T2D), have been suggested to link AD with T2D pathogenesis. Here, we show that constrained peptides designed to mimic the Aβ amyloid core (ACMs) are nanomolar cross-amyloid inhibitors of both IAPP and Aβ42 and effectively suppress reciprocal cross-seeding. Remarkably, ACMs act by co-assembling with IAPP or Aβ42 into amyloid fibril-resembling but non-toxic nanofibers and their highly ordered superstructures. Co-assembled nanofibers exhibit various potentially beneficial features including thermolability, proteolytic degradability, and effective cellular clearance which are reminiscent of labile/reversible functional amyloids. ACMs are thus promising leads for potent anti-amyloid drugs in both T2D and AD while the supramolecular nanofiber co-assemblies should inform the design of novel functional (hetero-)amyloid-based nanomaterials for biomedical/biotechnological applications. |
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| DOI: | doi:10.1038/s41467-022-32688-0 |
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| URL: | Bitte beachten Sie: Dies ist ein Bibliographieeintrag. Ein Volltextzugriff für Mitglieder der Universität besteht hier nur, falls für die entsprechende Zeitschrift/den entsprechenden Sammelband ein Abonnement besteht oder es sich um einen OpenAccess-Titel handelt.
Volltext ; Verlag: https://doi.org/10.1038/s41467-022-32688-0 |
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| | Volltext: https://www.nature.com/articles/s41467-022-32688-0 |
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| | DOI: https://doi.org/10.1038/s41467-022-32688-0 |
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| Datenträger: | Online-Ressource |
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| Sprache: | eng |
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| Sach-SW: | Alzheimer's disease |
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| | Peptides |
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| | Protein aggregation |
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| K10plus-PPN: | 182812639X |
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| Verknüpfungen: | → Zeitschrift |
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Designed peptides as nanomolar cross-amyloid inhibitors acting via supramolecular nanofiber co-assembly / Taş, Karin [VerfasserIn]; 25 August 2022 (Online-Ressource)
