A hydrophobic gold surface triggers misfolding and aggregation of the amyloidogenic Josephin domain in monomeric form, while leaving the oligomers unaffected.

Protein misfolding and aggregation in intracellular and extracellular spaces is regarded as a main marker of the presence of degenerative disorders such as amyloidoses. To elucidate the mechanisms of protein misfolding, the interaction of proteins with inorganic surfaces is of particular relevance,...

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Autores principales:	Alessandra Apicella, Monica Soncini, Marco Agostino Deriu, Antonino Natalello, Marcella Bonanomi, David Dellasega, Paolo Tortora, Maria Elena Regonesi, Carlo Spartaco Casari
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2013
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/d360e928f287454d920f4eb254314b10
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spelling	oai:doaj.org-article:d360e928f287454d920f4eb254314b102021-11-18T07:52:58ZA hydrophobic gold surface triggers misfolding and aggregation of the amyloidogenic Josephin domain in monomeric form, while leaving the oligomers unaffected.1932-620310.1371/journal.pone.0058794https://doaj.org/article/d360e928f287454d920f4eb254314b102013-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/23527026/?tool=EBIhttps://doaj.org/toc/1932-6203Protein misfolding and aggregation in intracellular and extracellular spaces is regarded as a main marker of the presence of degenerative disorders such as amyloidoses. To elucidate the mechanisms of protein misfolding, the interaction of proteins with inorganic surfaces is of particular relevance, since surfaces displaying different wettability properties may represent model systems of the cell membrane. Here, we unveil the role of surface hydrophobicity/hydrophilicity in the misfolding of the Josephin domain (JD), a globular-shaped domain of ataxin-3, the protein responsible for the spinocerebellar ataxia type 3. By means of a combined experimental and theoretical approach based on atomic force microscopy, Fourier transform infrared spectroscopy and molecular dynamics simulations, we reveal changes in JD morphology and secondary structure elicited by the interaction with the hydrophobic gold substrate, but not by the hydrophilic mica. Our results demonstrate that the interaction with the gold surface triggers misfolding of the JD when it is in native-like configuration, while no structural modification is observed after the protein has undergone oligomerization. This raises the possibility that biological membranes would be unable to affect amyloid oligomeric structures and toxicity.Alessandra ApicellaMonica SonciniMarco Agostino DeriuAntonino NatalelloMarcella BonanomiDavid DellasegaPaolo TortoraMaria Elena RegonesiCarlo Spartaco CasariPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 8, Iss 3, p e58794 (2013)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Alessandra Apicella Monica Soncini Marco Agostino Deriu Antonino Natalello Marcella Bonanomi David Dellasega Paolo Tortora Maria Elena Regonesi Carlo Spartaco Casari A hydrophobic gold surface triggers misfolding and aggregation of the amyloidogenic Josephin domain in monomeric form, while leaving the oligomers unaffected.
description	Protein misfolding and aggregation in intracellular and extracellular spaces is regarded as a main marker of the presence of degenerative disorders such as amyloidoses. To elucidate the mechanisms of protein misfolding, the interaction of proteins with inorganic surfaces is of particular relevance, since surfaces displaying different wettability properties may represent model systems of the cell membrane. Here, we unveil the role of surface hydrophobicity/hydrophilicity in the misfolding of the Josephin domain (JD), a globular-shaped domain of ataxin-3, the protein responsible for the spinocerebellar ataxia type 3. By means of a combined experimental and theoretical approach based on atomic force microscopy, Fourier transform infrared spectroscopy and molecular dynamics simulations, we reveal changes in JD morphology and secondary structure elicited by the interaction with the hydrophobic gold substrate, but not by the hydrophilic mica. Our results demonstrate that the interaction with the gold surface triggers misfolding of the JD when it is in native-like configuration, while no structural modification is observed after the protein has undergone oligomerization. This raises the possibility that biological membranes would be unable to affect amyloid oligomeric structures and toxicity.
format	article
author	Alessandra Apicella Monica Soncini Marco Agostino Deriu Antonino Natalello Marcella Bonanomi David Dellasega Paolo Tortora Maria Elena Regonesi Carlo Spartaco Casari
author_facet	Alessandra Apicella Monica Soncini Marco Agostino Deriu Antonino Natalello Marcella Bonanomi David Dellasega Paolo Tortora Maria Elena Regonesi Carlo Spartaco Casari
author_sort	Alessandra Apicella
title	A hydrophobic gold surface triggers misfolding and aggregation of the amyloidogenic Josephin domain in monomeric form, while leaving the oligomers unaffected.
title_short	A hydrophobic gold surface triggers misfolding and aggregation of the amyloidogenic Josephin domain in monomeric form, while leaving the oligomers unaffected.
title_full	A hydrophobic gold surface triggers misfolding and aggregation of the amyloidogenic Josephin domain in monomeric form, while leaving the oligomers unaffected.
title_fullStr	A hydrophobic gold surface triggers misfolding and aggregation of the amyloidogenic Josephin domain in monomeric form, while leaving the oligomers unaffected.
title_full_unstemmed	A hydrophobic gold surface triggers misfolding and aggregation of the amyloidogenic Josephin domain in monomeric form, while leaving the oligomers unaffected.
title_sort	hydrophobic gold surface triggers misfolding and aggregation of the amyloidogenic josephin domain in monomeric form, while leaving the oligomers unaffected.
publisher	Public Library of Science (PLoS)
publishDate	2013
url	https://doaj.org/article/d360e928f287454d920f4eb254314b10
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A hydrophobic gold surface triggers misfolding and aggregation of the amyloidogenic Josephin domain in monomeric form, while leaving the oligomers unaffected.

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