Competition between crystal and fibril formation in molecular mutations of amyloidogenic peptides

Aggregation of amyloidogenic peptides into fibrils and crystals has incidence in several amyloid-related diseases. Here, the authors investigate the origins of the fibril-to-crystal conversion in amyloidogenic hexapeptides pointing to the amyloid crystals as the ground state in the protein folding e...

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Main Authors:	Nicholas P. Reynolds, Jozef Adamcik, Joshua T. Berryman, Stephan Handschin, Ali Asghar Hakami Zanjani, Wen Li, Kun Liu, Afang Zhang, Raffaele Mezzenga
Format:	Article
Language:	English
Published:	Nature Publishing Group 2017-11-01
Series:	Nature Communications
Online Access:	https://doi.org/10.1038/s41467-017-01424-4

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spelling	doaj-f724699c0cff4d61b17cab20071aad412021-05-11T07:54:13ZengNature Publishing GroupNature Communications2041-17232017-11-018111010.1038/s41467-017-01424-4Competition between crystal and fibril formation in molecular mutations of amyloidogenic peptidesNicholas P. Reynolds0Jozef Adamcik1Joshua T. Berryman2Stephan Handschin3Ali Asghar Hakami Zanjani4Wen Li5Kun Liu6Afang Zhang7Raffaele Mezzenga8Swinburne University of Technology, ARC Training Centre for Biodevices, Faculty of Science, Engineering and TechnologyETH Zurich, Department of Health Sciences & TechnologyUniversity of Luxembourg, Department of Physics and Materials ScienceETH Zurich, Department of Health Sciences & TechnologyUniversity of Luxembourg, Department of Physics and Materials ScienceShanghai University, Department of Polymer MaterialsShanghai University, Department of Polymer MaterialsShanghai University, Department of Polymer MaterialsETH Zurich, Department of Health Sciences & TechnologyAggregation of amyloidogenic peptides into fibrils and crystals has incidence in several amyloid-related diseases. Here, the authors investigate the origins of the fibril-to-crystal conversion in amyloidogenic hexapeptides pointing to the amyloid crystals as the ground state in the protein folding energy landscape.https://doi.org/10.1038/s41467-017-01424-4
collection	DOAJ
language	English
format	Article
sources	DOAJ
author	Nicholas P. Reynolds Jozef Adamcik Joshua T. Berryman Stephan Handschin Ali Asghar Hakami Zanjani Wen Li Kun Liu Afang Zhang Raffaele Mezzenga
spellingShingle	Nicholas P. Reynolds Jozef Adamcik Joshua T. Berryman Stephan Handschin Ali Asghar Hakami Zanjani Wen Li Kun Liu Afang Zhang Raffaele Mezzenga Competition between crystal and fibril formation in molecular mutations of amyloidogenic peptides Nature Communications
author_facet	Nicholas P. Reynolds Jozef Adamcik Joshua T. Berryman Stephan Handschin Ali Asghar Hakami Zanjani Wen Li Kun Liu Afang Zhang Raffaele Mezzenga
author_sort	Nicholas P. Reynolds
title	Competition between crystal and fibril formation in molecular mutations of amyloidogenic peptides
title_short	Competition between crystal and fibril formation in molecular mutations of amyloidogenic peptides
title_full	Competition between crystal and fibril formation in molecular mutations of amyloidogenic peptides
title_fullStr	Competition between crystal and fibril formation in molecular mutations of amyloidogenic peptides
title_full_unstemmed	Competition between crystal and fibril formation in molecular mutations of amyloidogenic peptides
title_sort	competition between crystal and fibril formation in molecular mutations of amyloidogenic peptides
publisher	Nature Publishing Group
series	Nature Communications
issn	2041-1723
publishDate	2017-11-01
description	Aggregation of amyloidogenic peptides into fibrils and crystals has incidence in several amyloid-related diseases. Here, the authors investigate the origins of the fibril-to-crystal conversion in amyloidogenic hexapeptides pointing to the amyloid crystals as the ground state in the protein folding energy landscape.
url	https://doi.org/10.1038/s41467-017-01424-4
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Competition between crystal and fibril formation in molecular mutations of amyloidogenic peptides

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