Nanoscale studies link amyloid maturity with polyglutamine diseases onset

<p dir="ltr">The presence of expanded poly-glutamine (polyQ) repeats in proteins is directly linked to the pathogenesis of several neurodegenerative diseases, including Huntington’s disease. However, the molecular and structural basis underlying the increased toxicity of aggregates f...

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Main Author: F. S. Ruggeri (19738036) (author)
Other Authors: S. Vieweg (19738039) (author), U. Cendrowska (19738042) (author), G. Longo (19095992) (author), A. Chiki (19738045) (author), H. A. Lashuel (19738048) (author), G. Dietler (19738051) (author)
Published: 2016
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author F. S. Ruggeri (19738036)
author2 S. Vieweg (19738039)
U. Cendrowska (19738042)
G. Longo (19095992)
A. Chiki (19738045)
H. A. Lashuel (19738048)
G. Dietler (19738051)
author2_role author
author
author
author
author
author
author_facet F. S. Ruggeri (19738036)
S. Vieweg (19738039)
U. Cendrowska (19738042)
G. Longo (19095992)
A. Chiki (19738045)
H. A. Lashuel (19738048)
G. Dietler (19738051)
author_role author
dc.creator.none.fl_str_mv F. S. Ruggeri (19738036)
S. Vieweg (19738039)
U. Cendrowska (19738042)
G. Longo (19095992)
A. Chiki (19738045)
H. A. Lashuel (19738048)
G. Dietler (19738051)
dc.date.none.fl_str_mv 2016-08-08T03:00:00Z
dc.identifier.none.fl_str_mv 10.1038/srep31155
dc.relation.none.fl_str_mv https://figshare.com/articles/journal_contribution/Nanoscale_studies_link_amyloid_maturity_with_polyglutamine_diseases_onset/27101623
dc.rights.none.fl_str_mv CC BY 4.0
info:eu-repo/semantics/openAccess
dc.subject.none.fl_str_mv Biomedical and clinical sciences
Neurosciences
Huntington’s disease
Protein aggregation
Structural properties
Mechanical properties
Morphological properties
dc.title.none.fl_str_mv Nanoscale studies link amyloid maturity with polyglutamine diseases onset
dc.type.none.fl_str_mv Text
Journal contribution
info:eu-repo/semantics/publishedVersion
text
contribution to journal
description <p dir="ltr">The presence of expanded poly-glutamine (polyQ) repeats in proteins is directly linked to the pathogenesis of several neurodegenerative diseases, including Huntington’s disease. However, the molecular and structural basis underlying the increased toxicity of aggregates formed by proteins containing expanded polyQ repeats remain poorly understood, in part due to the size and morphological heterogeneity of the aggregates they form in vitro. To address this knowledge gap and technical limitations, we investigated the structural, mechanical and morphological properties of fibrillar aggregates at the single molecule and nanometer scale using the first exon of the Huntingtin protein as a model system (Exon1). Our findings demonstrate a direct correlation of the morphological and mechanical properties of Exon1 aggregates with their structural organization at the single aggregate and nanometric scale and provide novel insights into the molecular and structural basis of Huntingtin Exon1 aggregation and toxicity.</p><h2>Other Information</h2><p dir="ltr">Published in: Scientific Reports<br>License: <a href="https://creativecommons.org/licenses/by/4.0" target="_blank">https://creativecommons.org/licenses/by/4.0</a><br>See article on publisher's website: <a href="https://dx.doi.org/10.1038/srep31155" target="_blank">https://dx.doi.org/10.1038/srep31155</a></p>
eu_rights_str_mv openAccess
id Manara2_7ebc383e24e8d6dcc049acd2a5f54836
identifier_str_mv 10.1038/srep31155
network_acronym_str Manara2
network_name_str Manara2
oai_identifier_str oai:figshare.com:article/27101623
publishDate 2016
repository.mail.fl_str_mv
repository.name.fl_str_mv
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rights_invalid_str_mv CC BY 4.0
spelling Nanoscale studies link amyloid maturity with polyglutamine diseases onsetF. S. Ruggeri (19738036)S. Vieweg (19738039)U. Cendrowska (19738042)G. Longo (19095992)A. Chiki (19738045)H. A. Lashuel (19738048)G. Dietler (19738051)Biomedical and clinical sciencesNeurosciencesHuntington’s diseaseProtein aggregationStructural propertiesMechanical propertiesMorphological properties<p dir="ltr">The presence of expanded poly-glutamine (polyQ) repeats in proteins is directly linked to the pathogenesis of several neurodegenerative diseases, including Huntington’s disease. However, the molecular and structural basis underlying the increased toxicity of aggregates formed by proteins containing expanded polyQ repeats remain poorly understood, in part due to the size and morphological heterogeneity of the aggregates they form in vitro. To address this knowledge gap and technical limitations, we investigated the structural, mechanical and morphological properties of fibrillar aggregates at the single molecule and nanometer scale using the first exon of the Huntingtin protein as a model system (Exon1). Our findings demonstrate a direct correlation of the morphological and mechanical properties of Exon1 aggregates with their structural organization at the single aggregate and nanometric scale and provide novel insights into the molecular and structural basis of Huntingtin Exon1 aggregation and toxicity.</p><h2>Other Information</h2><p dir="ltr">Published in: Scientific Reports<br>License: <a href="https://creativecommons.org/licenses/by/4.0" target="_blank">https://creativecommons.org/licenses/by/4.0</a><br>See article on publisher's website: <a href="https://dx.doi.org/10.1038/srep31155" target="_blank">https://dx.doi.org/10.1038/srep31155</a></p>2016-08-08T03:00:00ZTextJournal contributioninfo:eu-repo/semantics/publishedVersiontextcontribution to journal10.1038/srep31155https://figshare.com/articles/journal_contribution/Nanoscale_studies_link_amyloid_maturity_with_polyglutamine_diseases_onset/27101623CC BY 4.0info:eu-repo/semantics/openAccessoai:figshare.com:article/271016232016-08-08T03:00:00Z
spellingShingle Nanoscale studies link amyloid maturity with polyglutamine diseases onset
F. S. Ruggeri (19738036)
Biomedical and clinical sciences
Neurosciences
Huntington’s disease
Protein aggregation
Structural properties
Mechanical properties
Morphological properties
status_str publishedVersion
title Nanoscale studies link amyloid maturity with polyglutamine diseases onset
title_full Nanoscale studies link amyloid maturity with polyglutamine diseases onset
title_fullStr Nanoscale studies link amyloid maturity with polyglutamine diseases onset
title_full_unstemmed Nanoscale studies link amyloid maturity with polyglutamine diseases onset
title_short Nanoscale studies link amyloid maturity with polyglutamine diseases onset
title_sort Nanoscale studies link amyloid maturity with polyglutamine diseases onset
topic Biomedical and clinical sciences
Neurosciences
Huntington’s disease
Protein aggregation
Structural properties
Mechanical properties
Morphological properties