Protein nanofibril design via manipulation of hydrogen bonds

How the structure of fibril-forming peptides influences the material and structural characteristics of their resultant assemblies remains an open question. Here, aliphatic to aromatic amino acid substitution in such peptides is shown to have little effect on the tendency to form amyloid-like fibrils...

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Autores principales:	Nidhi Aggarwal, Dror Eliaz, Hagai Cohen, Irit Rosenhek-Goldian, Sidney R. Cohen, Anna Kozell, Thomas O. Mason, Ulyana Shimanovich
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Chemistry QD1-999
Acceso en línea:	https://doaj.org/article/54817c4a122e4f69b2e18a9f88413568
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spelling	oai:doaj.org-article:54817c4a122e4f69b2e18a9f884135682021-12-02T14:35:32ZProtein nanofibril design via manipulation of hydrogen bonds10.1038/s42004-021-00494-22399-3669https://doaj.org/article/54817c4a122e4f69b2e18a9f884135682021-05-01T00:00:00Zhttps://doi.org/10.1038/s42004-021-00494-2https://doaj.org/toc/2399-3669How the structure of fibril-forming peptides influences the material and structural characteristics of their resultant assemblies remains an open question. Here, aliphatic to aromatic amino acid substitution in such peptides is shown to have little effect on the tendency to form amyloid-like fibrils, but instead alters the pathway by which they form and the mechanical properties of peptide supramolecular assemblies.Nidhi AggarwalDror EliazHagai CohenIrit Rosenhek-GoldianSidney R. CohenAnna KozellThomas O. MasonUlyana ShimanovichNature PortfolioarticleChemistryQD1-999ENCommunications Chemistry, Vol 4, Iss 1, Pp 1-10 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Chemistry QD1-999
spellingShingle	Chemistry QD1-999 Nidhi Aggarwal Dror Eliaz Hagai Cohen Irit Rosenhek-Goldian Sidney R. Cohen Anna Kozell Thomas O. Mason Ulyana Shimanovich Protein nanofibril design via manipulation of hydrogen bonds
description	How the structure of fibril-forming peptides influences the material and structural characteristics of their resultant assemblies remains an open question. Here, aliphatic to aromatic amino acid substitution in such peptides is shown to have little effect on the tendency to form amyloid-like fibrils, but instead alters the pathway by which they form and the mechanical properties of peptide supramolecular assemblies.
format	article
author	Nidhi Aggarwal Dror Eliaz Hagai Cohen Irit Rosenhek-Goldian Sidney R. Cohen Anna Kozell Thomas O. Mason Ulyana Shimanovich
author_facet	Nidhi Aggarwal Dror Eliaz Hagai Cohen Irit Rosenhek-Goldian Sidney R. Cohen Anna Kozell Thomas O. Mason Ulyana Shimanovich
author_sort	Nidhi Aggarwal
title	Protein nanofibril design via manipulation of hydrogen bonds
title_short	Protein nanofibril design via manipulation of hydrogen bonds
title_full	Protein nanofibril design via manipulation of hydrogen bonds
title_fullStr	Protein nanofibril design via manipulation of hydrogen bonds
title_full_unstemmed	Protein nanofibril design via manipulation of hydrogen bonds
title_sort	protein nanofibril design via manipulation of hydrogen bonds
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/54817c4a122e4f69b2e18a9f88413568
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Protein nanofibril design via manipulation of hydrogen bonds

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