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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Autores principales:	Nicholas P. Reynolds, Jozef Adamcik, Joshua T. Berryman, Stephan Handschin, Ali Asghar Hakami Zanjani, Wen Li, Kun Liu, Afang Zhang, Raffaele Mezzenga
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/f724699c0cff4d61b17cab20071aad41
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spelling	oai:doaj.org-article:f724699c0cff4d61b17cab20071aad412021-12-02T14:41:11ZCompetition between crystal and fibril formation in molecular mutations of amyloidogenic peptides10.1038/s41467-017-01424-42041-1723https://doaj.org/article/f724699c0cff4d61b17cab20071aad412017-11-01T00:00:00Zhttps://doi.org/10.1038/s41467-017-01424-4https://doaj.org/toc/2041-1723Aggregation 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.Nicholas P. ReynoldsJozef AdamcikJoshua T. BerrymanStephan HandschinAli Asghar Hakami ZanjaniWen LiKun LiuAfang ZhangRaffaele MezzengaNature PortfolioarticleScienceQENNature Communications, Vol 8, Iss 1, Pp 1-10 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q 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
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.
format	article
author	Nicholas P. Reynolds Jozef Adamcik Joshua T. Berryman Stephan Handschin Ali Asghar Hakami Zanjani Wen Li Kun Liu Afang Zhang Raffaele Mezzenga
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 Portfolio
publishDate	2017
url	https://doaj.org/article/f724699c0cff4d61b17cab20071aad41
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Competition between crystal and fibril formation in molecular mutations of amyloidogenic peptides

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