Amyloids in solid-state nuclear magnetic resonance: potential causes of the usually low resolution

Alba Espargaró, Maria Antònia Busquets, Joan Estelrich, Raimon Sabate Department of Physical Chemistry, School of Pharmacy, Institute of Nanoscience and Nanotechnology (IN2UB), University of Barcelona, Barcelona, Spain Abstract: Amyloids are non-crystalline and insoluble, whi...

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Autores principales:	Espargaró A, Busquets MA, Estelrich J, Sabate R
Formato:	article
Lenguaje:	EN
Publicado:	Dove Medical Press 2015
Materias:	Medicine (General) R5-920
Acceso en línea:	https://doaj.org/article/66182d88a1dc46f7895e55e57dce50c1
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spelling	oai:doaj.org-article:66182d88a1dc46f7895e55e57dce50c12021-12-02T03:55:34ZAmyloids in solid-state nuclear magnetic resonance: potential causes of the usually low resolution1178-2013https://doaj.org/article/66182d88a1dc46f7895e55e57dce50c12015-11-01T00:00:00Zhttps://www.dovepress.com/amyloids-in-solid-state-nuclear-magnetic-resonance-potential-causes-of-peer-reviewed-article-IJNhttps://doaj.org/toc/1178-2013Alba Espargaró, Maria Antònia Busquets, Joan Estelrich, Raimon Sabate Department of Physical Chemistry, School of Pharmacy, Institute of Nanoscience and Nanotechnology (IN2UB), University of Barcelona, Barcelona, Spain Abstract: Amyloids are non-crystalline and insoluble, which imply that the classical structural biology tools, ie, X-ray crystallography and solution nuclear magnetic resonance (NMR), are not suitable for their analysis. In the last years, solid-state NMR (ssNMR) has emerged as an alternative tool to decrypt the structural signatures of amyloid fibrils, providing major contributions to our understanding of molecular structures of amyloids such as β-amyloid peptide associated with Alzheimer’s disease or fungal prions, among others. Despite this, the wide majority of amyloid fibrils display low resolution by ssNMR. Usually, this low resolution has been attributed to a high disorder or polymorphism of the fibrils, suggesting the existence of diverse elementary β-sheet structures. Here, we propose that a single β-sheet structure could be responsible for the broadening of the line widths in the ssNMR spectra. Although the fibrils and fibers consist of a single elementary structure, the angle of twist of each individual fibril in the mature fiber depends on the number of individual fibrils as well as the fibril arrangement in the final mature fiber. Thus, a wide range of angles of twist could be observed in the same amyloid sample. These twist variations involve changes in amino acid alignments that could be enough to limit the ssNMR resolution. Keywords: amyloid, fibril, misfolding, β-structure, ssNMR, NMR, β-sheetEspargaró ABusquets MAEstelrich JSabate RDove Medical PressarticleMedicine (General)R5-920ENInternational Journal of Nanomedicine, Vol 2015, Iss default, Pp 6975-6983 (2015)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine (General) R5-920
spellingShingle	Medicine (General) R5-920 Espargaró A Busquets MA Estelrich J Sabate R Amyloids in solid-state nuclear magnetic resonance: potential causes of the usually low resolution
description	Alba Espargaró, Maria Antònia Busquets, Joan Estelrich, Raimon Sabate Department of Physical Chemistry, School of Pharmacy, Institute of Nanoscience and Nanotechnology (IN2UB), University of Barcelona, Barcelona, Spain Abstract: Amyloids are non-crystalline and insoluble, which imply that the classical structural biology tools, ie, X-ray crystallography and solution nuclear magnetic resonance (NMR), are not suitable for their analysis. In the last years, solid-state NMR (ssNMR) has emerged as an alternative tool to decrypt the structural signatures of amyloid fibrils, providing major contributions to our understanding of molecular structures of amyloids such as β-amyloid peptide associated with Alzheimer’s disease or fungal prions, among others. Despite this, the wide majority of amyloid fibrils display low resolution by ssNMR. Usually, this low resolution has been attributed to a high disorder or polymorphism of the fibrils, suggesting the existence of diverse elementary β-sheet structures. Here, we propose that a single β-sheet structure could be responsible for the broadening of the line widths in the ssNMR spectra. Although the fibrils and fibers consist of a single elementary structure, the angle of twist of each individual fibril in the mature fiber depends on the number of individual fibrils as well as the fibril arrangement in the final mature fiber. Thus, a wide range of angles of twist could be observed in the same amyloid sample. These twist variations involve changes in amino acid alignments that could be enough to limit the ssNMR resolution. Keywords: amyloid, fibril, misfolding, β-structure, ssNMR, NMR, β-sheet
format	article
author	Espargaró A Busquets MA Estelrich J Sabate R
author_facet	Espargaró A Busquets MA Estelrich J Sabate R
author_sort	Espargaró A
title	Amyloids in solid-state nuclear magnetic resonance: potential causes of the usually low resolution
title_short	Amyloids in solid-state nuclear magnetic resonance: potential causes of the usually low resolution
title_full	Amyloids in solid-state nuclear magnetic resonance: potential causes of the usually low resolution
title_fullStr	Amyloids in solid-state nuclear magnetic resonance: potential causes of the usually low resolution
title_full_unstemmed	Amyloids in solid-state nuclear magnetic resonance: potential causes of the usually low resolution
title_sort	amyloids in solid-state nuclear magnetic resonance: potential causes of the usually low resolution
publisher	Dove Medical Press
publishDate	2015
url	https://doaj.org/article/66182d88a1dc46f7895e55e57dce50c1
work_keys_str_mv	AT espargaroa amyloidsinsolidstatenuclearmagneticresonancepotentialcausesoftheusuallylowresolution AT busquetsma amyloidsinsolidstatenuclearmagneticresonancepotentialcausesoftheusuallylowresolution AT estelrichj amyloidsinsolidstatenuclearmagneticresonancepotentialcausesoftheusuallylowresolution AT sabater amyloidsinsolidstatenuclearmagneticresonancepotentialcausesoftheusuallylowresolution
_version_	1718401552511664128

Amyloids in solid-state nuclear magnetic resonance: potential causes of the usually low resolution

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