Designed peptides as nanomolar cross-amyloid inhibitors acting via supramolecular nanofiber co-assembly
Amyloid self-assembly is linked to type 2 diabetes and Alzheimer’s disease. Here the authors designed constrained peptides which are nanomolar amyloid inhibitors of the key polypeptides IAPP and Aβ42 and act via supramolecular nanofiber co-assembly.
Main Authors: | , , , , , , , , , , , , , , , , , |
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Format: | Article |
Language: | English |
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Nature Portfolio
2022-08-01
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Series: | Nature Communications |
Online Access: | https://doi.org/10.1038/s41467-022-32688-0 |
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author | 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 |
author_facet | 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 |
author_sort | Karin Taş |
collection | DOAJ |
description | Amyloid self-assembly is linked to type 2 diabetes and Alzheimer’s disease. Here the authors designed constrained peptides which are nanomolar amyloid inhibitors of the key polypeptides IAPP and Aβ42 and act via supramolecular nanofiber co-assembly. |
first_indexed | 2024-04-13T02:50:19Z |
format | Article |
id | doaj.art-3b23585f88cb4b29866249912e9885cc |
institution | Directory Open Access Journal |
issn | 2041-1723 |
language | English |
last_indexed | 2024-04-13T02:50:19Z |
publishDate | 2022-08-01 |
publisher | Nature Portfolio |
record_format | Article |
series | Nature Communications |
spelling | doaj.art-3b23585f88cb4b29866249912e9885cc2022-12-22T03:05:52ZengNature PortfolioNature Communications2041-17232022-08-0113112210.1038/s41467-022-32688-0Designed peptides as nanomolar cross-amyloid inhibitors acting via supramolecular nanofiber co-assemblyKarin Taş0Beatrice Dalla Volta1Christina Lindner2Omar El Bounkari3Kathleen Hille4Yuan Tian5Xènia Puig-Bosch6Markus Ballmann7Simon Hornung8Martin Ortner9Sophia Prem10Laura Meier11Gerhard Rammes12Martin Haslbeck13Christian Weber14Remco T. A. Megens15Jürgen Bernhagen16Aphrodite Kapurniotu17Division of Peptide Biochemistry, TUM School of Life Sciences, Technical University of Munich (TUM)Division of Peptide Biochemistry, TUM School of Life Sciences, Technical University of Munich (TUM)Division of Peptide Biochemistry, TUM School of Life Sciences, Technical University of Munich (TUM)Division of Vascular Biology, Institute for Stroke and Dementia Research (ISD), Klinikum der Universität München, Ludwig-Maximilian-University (LMU)Division of Peptide Biochemistry, TUM School of Life Sciences, Technical University of Munich (TUM)Division of Vascular Biology, Institute for Stroke and Dementia Research (ISD), Klinikum der Universität München, Ludwig-Maximilian-University (LMU)Department of Anesthesiology and Intensive Care, Technical University of Munich/Klinikum Rechts der IsarDepartment of Anesthesiology and Intensive Care, Technical University of Munich/Klinikum Rechts der IsarDivision of Peptide Biochemistry, TUM School of Life Sciences, Technical University of Munich (TUM)Division of Peptide Biochemistry, TUM School of Life Sciences, Technical University of Munich (TUM)Division of Peptide Biochemistry, TUM School of Life Sciences, Technical University of Munich (TUM)Center for Protein Assemblies, Department of Chemistry, Technical University of MunichDepartment of Anesthesiology and Intensive Care, Technical University of Munich/Klinikum Rechts der IsarCenter for Protein Assemblies, Department of Chemistry, Technical University of MunichInstitute for Cardiovascular Prevention, Klinikum der Universität München, Ludwig-Maximilian-University Munich (LMU)Institute for Cardiovascular Prevention, Klinikum der Universität München, Ludwig-Maximilian-University Munich (LMU)Division of Vascular Biology, Institute for Stroke and Dementia Research (ISD), Klinikum der Universität München, Ludwig-Maximilian-University (LMU)Division of Peptide Biochemistry, TUM School of Life Sciences, Technical University of Munich (TUM)Amyloid self-assembly is linked to type 2 diabetes and Alzheimer’s disease. Here the authors designed constrained peptides which are nanomolar amyloid inhibitors of the key polypeptides IAPP and Aβ42 and act via supramolecular nanofiber co-assembly.https://doi.org/10.1038/s41467-022-32688-0 |
spellingShingle | 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 Designed peptides as nanomolar cross-amyloid inhibitors acting via supramolecular nanofiber co-assembly Nature Communications |
title | Designed peptides as nanomolar cross-amyloid inhibitors acting via supramolecular nanofiber co-assembly |
title_full | Designed peptides as nanomolar cross-amyloid inhibitors acting via supramolecular nanofiber co-assembly |
title_fullStr | Designed peptides as nanomolar cross-amyloid inhibitors acting via supramolecular nanofiber co-assembly |
title_full_unstemmed | Designed peptides as nanomolar cross-amyloid inhibitors acting via supramolecular nanofiber co-assembly |
title_short | Designed peptides as nanomolar cross-amyloid inhibitors acting via supramolecular nanofiber co-assembly |
title_sort | designed peptides as nanomolar cross amyloid inhibitors acting via supramolecular nanofiber co assembly |
url | https://doi.org/10.1038/s41467-022-32688-0 |
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