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.

Bibliographic Details
Main Authors: 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
Format: Article
Language:English
Published: Nature Portfolio 2022-08-01
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.
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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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