Infrared nanospectroscopy reveals the molecular interaction fingerprint of an aggregation inhibitor with single Aβ42 oligomers

Our understanding of the molecular mechanisms underlying pathological protein aggregation remains incomplete. Here, single molecule infrared nanospectroscopy (AFM-IR) offers insight into the structure of Aβ42 oligomeric and fibrillar species and their interaction with an aggregation inhibitor, pavin...

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Autores principales:	Francesco Simone Ruggeri, Johnny Habchi, Sean Chia, Robert I. Horne, Michele Vendruscolo, Tuomas P. J. Knowles
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/7f8ac1eb0b6149b48b24e7005907776f
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spelling	oai:doaj.org-article:7f8ac1eb0b6149b48b24e7005907776f2021-12-02T13:27:30ZInfrared nanospectroscopy reveals the molecular interaction fingerprint of an aggregation inhibitor with single Aβ42 oligomers10.1038/s41467-020-20782-02041-1723https://doaj.org/article/7f8ac1eb0b6149b48b24e7005907776f2021-01-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-20782-0https://doaj.org/toc/2041-1723Our understanding of the molecular mechanisms underlying pathological protein aggregation remains incomplete. Here, single molecule infrared nanospectroscopy (AFM-IR) offers insight into the structure of Aβ42 oligomeric and fibrillar species and their interaction with an aggregation inhibitor, paving the way for single molecule drug discovery studies.Francesco Simone RuggeriJohnny HabchiSean ChiaRobert I. HorneMichele VendruscoloTuomas P. J. KnowlesNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-9 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Francesco Simone Ruggeri Johnny Habchi Sean Chia Robert I. Horne Michele Vendruscolo Tuomas P. J. Knowles Infrared nanospectroscopy reveals the molecular interaction fingerprint of an aggregation inhibitor with single Aβ42 oligomers
description	Our understanding of the molecular mechanisms underlying pathological protein aggregation remains incomplete. Here, single molecule infrared nanospectroscopy (AFM-IR) offers insight into the structure of Aβ42 oligomeric and fibrillar species and their interaction with an aggregation inhibitor, paving the way for single molecule drug discovery studies.
format	article
author	Francesco Simone Ruggeri Johnny Habchi Sean Chia Robert I. Horne Michele Vendruscolo Tuomas P. J. Knowles
author_facet	Francesco Simone Ruggeri Johnny Habchi Sean Chia Robert I. Horne Michele Vendruscolo Tuomas P. J. Knowles
author_sort	Francesco Simone Ruggeri
title	Infrared nanospectroscopy reveals the molecular interaction fingerprint of an aggregation inhibitor with single Aβ42 oligomers
title_short	Infrared nanospectroscopy reveals the molecular interaction fingerprint of an aggregation inhibitor with single Aβ42 oligomers
title_full	Infrared nanospectroscopy reveals the molecular interaction fingerprint of an aggregation inhibitor with single Aβ42 oligomers
title_fullStr	Infrared nanospectroscopy reveals the molecular interaction fingerprint of an aggregation inhibitor with single Aβ42 oligomers
title_full_unstemmed	Infrared nanospectroscopy reveals the molecular interaction fingerprint of an aggregation inhibitor with single Aβ42 oligomers
title_sort	infrared nanospectroscopy reveals the molecular interaction fingerprint of an aggregation inhibitor with single aβ42 oligomers
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/7f8ac1eb0b6149b48b24e7005907776f
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Infrared nanospectroscopy reveals the molecular interaction fingerprint of an aggregation inhibitor with single Aβ42 oligomers

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