Designed peptides as nanomolar cross-amyloid inhibitors acting via supramolecular nanofiber co-assembly
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)...
Saved in:
| Main Authors: | , , , , , , , , , , , , , , , , , |
|---|---|
| Format: | Article (Journal) |
| Language: | English |
| Published: |
25 August 2022
|
| In: |
Nature Communications
Year: 2022, Volume: 13, Pages: 1-22 |
| ISSN: | 2041-1723 |
| DOI: | 10.1038/s41467-022-32688-0 |
| Online Access: | Resolving-System, lizenzpflichtig, Volltext: https://doi.org/10.1038/s41467-022-32688-0 Verlag, lizenzpflichtig, Volltext: https://www.nature.com/articles/s41467-022-32688-0 
|
| Author Notes: | 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 |
MARC
| LEADER | 00000caa a2200000 c 4500 | ||
|---|---|---|---|
| 001 | 182812639X | ||
| 003 | DE-627 | ||
| 005 | 20230426192846.0 | ||
| 007 | cr uuu---uuuuu | ||
| 008 | 221220s2022 xx |||||o 00| ||eng c | ||
| 024 | 7 | |a 10.1038/s41467-022-32688-0 |2 doi | |
| 035 | |a (DE-627)182812639X | ||
| 035 | |a (DE-599)KXP182812639X | ||
| 035 | |a (OCoLC)1361670164 | ||
| 040 | |a DE-627 |b ger |c DE-627 |e rda | ||
| 041 | |a eng | ||
| 084 | |a 30 |2 sdnb | ||
| 100 | 1 | |a Taş, Karin |e VerfasserIn |0 (DE-588)1276167466 |0 (DE-627)1828129151 |4 aut | |
| 245 | 1 | 0 | |a Designed peptides as nanomolar cross-amyloid inhibitors acting via supramolecular nanofiber co-assembly |c 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 |
| 264 | 1 | |c 25 August 2022 | |
| 300 | |a 22 | ||
| 336 | |a Text |b txt |2 rdacontent | ||
| 337 | |a Computermedien |b c |2 rdamedia | ||
| 338 | |a Online-Ressource |b cr |2 rdacarrier | ||
| 500 | |a Gesehen am 20.12.2022 | ||
| 520 | |a 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. | ||
| 650 | 4 | |a Alzheimer's disease | |
| 650 | 4 | |a Peptides | |
| 650 | 4 | |a Protein aggregation | |
| 700 | 1 | |a Volta, Beatrice Dalla |e VerfasserIn |4 aut | |
| 700 | 1 | |a Lindner, Christina |d 1994- |e VerfasserIn |0 (DE-588)1276166567 |0 (DE-627)1828127191 |4 aut | |
| 700 | 1 | |a El Bounkari, Omar |e VerfasserIn |4 aut | |
| 700 | 1 | |a Hille, Kathleen |e VerfasserIn |4 aut | |
| 700 | 1 | |a Tian, Yuan |e VerfasserIn |4 aut | |
| 700 | 1 | |a Puig-Bosch, Xènia |e VerfasserIn |4 aut | |
| 700 | 1 | |a Ballmann, Markus |e VerfasserIn |4 aut | |
| 700 | 1 | |a Hornung, Simon |e VerfasserIn |4 aut | |
| 700 | 1 | |a Ortner, Martin |e VerfasserIn |4 aut | |
| 700 | 1 | |a Prem, Sophia |e VerfasserIn |4 aut | |
| 700 | 1 | |a Meier, Laura |e VerfasserIn |4 aut | |
| 700 | 1 | |a Rammes, Gerhard |e VerfasserIn |4 aut | |
| 700 | 1 | |a Haslbeck, Martin |e VerfasserIn |4 aut | |
| 700 | 1 | |a Weber, Christian |e VerfasserIn |4 aut | |
| 700 | 1 | |a Megens, Remco T. A. |e VerfasserIn |4 aut | |
| 700 | 1 | |a Bernhagen, Jürgen |e VerfasserIn |4 aut | |
| 700 | 1 | |a Kapurniotu, Aphrodite |e VerfasserIn |4 aut | |
| 773 | 0 | 8 | |i Enthalten in |t Nature Communications |d [London] : Springer Nature, 2010 |g 13(2022), Artikel-ID 5004, Seite 1-22 |h Online-Ressource |w (DE-627)626457688 |w (DE-600)2553671-0 |w (DE-576)331555905 |x 2041-1723 |7 nnas |a Designed peptides as nanomolar cross-amyloid inhibitors acting via supramolecular nanofiber co-assembly |
| 773 | 1 | 8 | |g volume:13 |g year:2022 |g elocationid:5004 |g pages:1-22 |g extent:22 |a Designed peptides as nanomolar cross-amyloid inhibitors acting via supramolecular nanofiber co-assembly |
| 856 | 4 | 0 | |u https://doi.org/10.1038/s41467-022-32688-0 |x Resolving-System |x Verlag |z lizenzpflichtig |3 Volltext |
| 856 | 4 | 0 | |u https://www.nature.com/articles/s41467-022-32688-0 |x Verlag |z lizenzpflichtig |3 Volltext |
| 951 | |a AR | ||
| 992 | |a 20221220 | ||
| 993 | |a Article | ||
| 994 | |a 2022 | ||
| 998 | |g 1276166567 |a Lindner, Christina |m 1276166567:Lindner, Christina |d 120000 |d 120100 |e 120000PL1276166567 |e 120100PL1276166567 |k 0/120000/ |k 1/120000/120100/ |p 3 | ||
| 999 | |a KXP-PPN182812639X |e 4235951890 | ||
| BIB | |a Y | ||
| SER | |a journal | ||
| JSO | |a {"recId":"182812639X","language":["eng"],"note":["Gesehen am 20.12.2022"],"type":{"bibl":"article-journal","media":"Online-Ressource"},"person":[{"roleDisplay":"VerfasserIn","display":"Taş, Karin","role":"aut","family":"Taş","given":"Karin"},{"display":"Volta, Beatrice Dalla","roleDisplay":"VerfasserIn","role":"aut","family":"Volta","given":"Beatrice Dalla"},{"role":"aut","roleDisplay":"VerfasserIn","display":"Lindner, Christina","given":"Christina","family":"Lindner"},{"role":"aut","roleDisplay":"VerfasserIn","display":"El Bounkari, Omar","given":"Omar","family":"El Bounkari"},{"given":"Kathleen","family":"Hille","role":"aut","display":"Hille, Kathleen","roleDisplay":"VerfasserIn"},{"role":"aut","display":"Tian, Yuan","roleDisplay":"VerfasserIn","given":"Yuan","family":"Tian"},{"display":"Puig-Bosch, Xènia","roleDisplay":"VerfasserIn","role":"aut","family":"Puig-Bosch","given":"Xènia"},{"role":"aut","roleDisplay":"VerfasserIn","display":"Ballmann, Markus","given":"Markus","family":"Ballmann"},{"given":"Simon","family":"Hornung","role":"aut","roleDisplay":"VerfasserIn","display":"Hornung, Simon"},{"roleDisplay":"VerfasserIn","display":"Ortner, Martin","role":"aut","family":"Ortner","given":"Martin"},{"family":"Prem","given":"Sophia","roleDisplay":"VerfasserIn","display":"Prem, Sophia","role":"aut"},{"role":"aut","roleDisplay":"VerfasserIn","display":"Meier, Laura","given":"Laura","family":"Meier"},{"family":"Rammes","given":"Gerhard","display":"Rammes, Gerhard","roleDisplay":"VerfasserIn","role":"aut"},{"role":"aut","display":"Haslbeck, Martin","roleDisplay":"VerfasserIn","given":"Martin","family":"Haslbeck"},{"display":"Weber, Christian","roleDisplay":"VerfasserIn","role":"aut","family":"Weber","given":"Christian"},{"role":"aut","display":"Megens, Remco T. A.","roleDisplay":"VerfasserIn","given":"Remco T. A.","family":"Megens"},{"given":"Jürgen","family":"Bernhagen","role":"aut","display":"Bernhagen, Jürgen","roleDisplay":"VerfasserIn"},{"given":"Aphrodite","family":"Kapurniotu","role":"aut","roleDisplay":"VerfasserIn","display":"Kapurniotu, Aphrodite"}],"title":[{"title_sort":"Designed peptides as nanomolar cross-amyloid inhibitors acting via supramolecular nanofiber co-assembly","title":"Designed peptides as nanomolar cross-amyloid inhibitors acting via supramolecular nanofiber co-assembly"}],"relHost":[{"id":{"issn":["2041-1723"],"zdb":["2553671-0"],"eki":["626457688"]},"origin":[{"publisherPlace":"[London] ; [London]","dateIssuedDisp":"[2010]-","publisher":"Springer Nature ; Nature Publishing Group UK"}],"physDesc":[{"extent":"Online-Ressource"}],"title":[{"title_sort":"Nature Communications","title":"Nature Communications"}],"part":{"year":"2022","pages":"1-22","text":"13(2022), Artikel-ID 5004, Seite 1-22","volume":"13","extent":"22"},"pubHistory":["2010-"],"language":["eng"],"recId":"626457688","type":{"bibl":"periodical","media":"Online-Ressource"},"note":["Gesehen am 13.06.24"],"disp":"Designed peptides as nanomolar cross-amyloid inhibitors acting via supramolecular nanofiber co-assemblyNature Communications"}],"physDesc":[{"extent":"22 S."}],"name":{"displayForm":["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"]},"id":{"doi":["10.1038/s41467-022-32688-0"],"eki":["182812639X"]},"origin":[{"dateIssuedDisp":"25 August 2022","dateIssuedKey":"2022"}]} | ||
| SRT | |a TASKARINVODESIGNEDPE2520 | ||