A condensation-ordering mechanism in nanoparticle-catalyzed peptide aggregation.

Nanoparticles introduced in living cells are capable of strongly promoting the aggregation of peptides and proteins. We use here molecular dynamics simulations to characterise in detail the process by which nanoparticle surfaces catalyse the self-assembly of peptides into fibrillar structures. The s...

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Autores principales:	Stefan Auer, Antonio Trovato, Michele Vendruscolo
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2009
Materias:	Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/dc970ccdd8e741279e51502d8322fa5d
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spelling	oai:doaj.org-article:dc970ccdd8e741279e51502d8322fa5d2021-11-25T05:42:14ZA condensation-ordering mechanism in nanoparticle-catalyzed peptide aggregation.1553-734X1553-735810.1371/journal.pcbi.1000458https://doaj.org/article/dc970ccdd8e741279e51502d8322fa5d2009-08-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/19680431/pdf/?tool=EBIhttps://doaj.org/toc/1553-734Xhttps://doaj.org/toc/1553-7358Nanoparticles introduced in living cells are capable of strongly promoting the aggregation of peptides and proteins. We use here molecular dynamics simulations to characterise in detail the process by which nanoparticle surfaces catalyse the self-assembly of peptides into fibrillar structures. The simulation of a system of hundreds of peptides over the millisecond timescale enables us to show that the mechanism of aggregation involves a first phase in which small structurally disordered oligomers assemble onto the nanoparticle and a second phase in which they evolve into highly ordered as their size increases.Stefan AuerAntonio TrovatoMichele VendruscoloPublic Library of Science (PLoS)articleBiology (General)QH301-705.5ENPLoS Computational Biology, Vol 5, Iss 8, p e1000458 (2009)
institution	DOAJ
collection	DOAJ
language	EN
topic	Biology (General) QH301-705.5
spellingShingle	Biology (General) QH301-705.5 Stefan Auer Antonio Trovato Michele Vendruscolo A condensation-ordering mechanism in nanoparticle-catalyzed peptide aggregation.
description	Nanoparticles introduced in living cells are capable of strongly promoting the aggregation of peptides and proteins. We use here molecular dynamics simulations to characterise in detail the process by which nanoparticle surfaces catalyse the self-assembly of peptides into fibrillar structures. The simulation of a system of hundreds of peptides over the millisecond timescale enables us to show that the mechanism of aggregation involves a first phase in which small structurally disordered oligomers assemble onto the nanoparticle and a second phase in which they evolve into highly ordered as their size increases.
format	article
author	Stefan Auer Antonio Trovato Michele Vendruscolo
author_facet	Stefan Auer Antonio Trovato Michele Vendruscolo
author_sort	Stefan Auer
title	A condensation-ordering mechanism in nanoparticle-catalyzed peptide aggregation.
title_short	A condensation-ordering mechanism in nanoparticle-catalyzed peptide aggregation.
title_full	A condensation-ordering mechanism in nanoparticle-catalyzed peptide aggregation.
title_fullStr	A condensation-ordering mechanism in nanoparticle-catalyzed peptide aggregation.
title_full_unstemmed	A condensation-ordering mechanism in nanoparticle-catalyzed peptide aggregation.
title_sort	condensation-ordering mechanism in nanoparticle-catalyzed peptide aggregation.
publisher	Public Library of Science (PLoS)
publishDate	2009
url	https://doaj.org/article/dc970ccdd8e741279e51502d8322fa5d
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A condensation-ordering mechanism in nanoparticle-catalyzed peptide aggregation.

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