| Online-Ressource |
Verfasst von: | Taş, Karin [VerfasserIn]  |
| Volta, Beatrice Dalla [VerfasserIn]  |
| Lindner, Christina [VerfasserIn]  |
| El Bounkari, Omar [VerfasserIn]  |
| Hille, Kathleen [VerfasserIn]  |
| Tian, Yuan [VerfasserIn]  |
| Puig-Bosch, Xènia [VerfasserIn]  |
| Ballmann, Markus [VerfasserIn]  |
| Hornung, Simon [VerfasserIn]  |
| Ortner, Martin [VerfasserIn]  |
| Prem, Sophia [VerfasserIn]  |
| Meier, Laura [VerfasserIn]  |
| Rammes, Gerhard [VerfasserIn]  |
| Haslbeck, Martin [VerfasserIn]  |
| Weber, Christian [VerfasserIn]  |
| Megens, Remco T. A. [VerfasserIn]  |
| Bernhagen, Jürgen [VerfasserIn]  |
| Kapurniotu, Aphrodite [VerfasserIn]  |
Titel: | Designed peptides as nanomolar cross-amyloid inhibitors acting via supramolecular nanofiber co-assembly |
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 |
E-Jahr: | 2022 |
Jahr: | 25 August 2022 |
Umfang: | 22 S. |
Fussnoten: | Gesehen am 20.12.2022 |
Titel Quelle: | Enthalten in: Nature Communications |
Ort Quelle: | [London] : Nature Publishing Group UK, 2010 |
Jahr Quelle: | 2022 |
Band/Heft Quelle: | 13(2022), Artikel-ID 5004, Seite 1-22 |
ISSN Quelle: | 2041-1723 |
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. |
DOI: | doi:10.1038/s41467-022-32688-0 |
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 |
| Volltext: https://www.nature.com/articles/s41467-022-32688-0 |
| DOI: https://doi.org/10.1038/s41467-022-32688-0 |
Datenträger: | Online-Ressource |
Sprache: | eng |
Sach-SW: | Alzheimer's disease |
| Peptides |
| Protein aggregation |
K10plus-PPN: | 182812639X |
Verknüpfungen: | → Zeitschrift |
Designed peptides as nanomolar cross-amyloid inhibitors acting via supramolecular nanofiber co-assembly / Taş, Karin [VerfasserIn]; 25 August 2022 (Online-Ressource)