Interaction of β-sheet folds with a gold surface.

The adsorption of proteins on inorganic surfaces is of fundamental biological importance. Further, biomedical and nanotechnological applications increasingly use interfaces between inorganic material and polypeptides. Yet, the underlying adsorption mechanism of polypeptides on surfaces is not well u...

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Autores principales:	Martin Hoefling, Susanna Monti, Stefano Corni, Kay Eberhard Gottschalk
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2011
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/1f9276bfc09842bba7f5d5e2ae678062
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spelling	oai:doaj.org-article:1f9276bfc09842bba7f5d5e2ae6780622021-11-18T06:52:29ZInteraction of β-sheet folds with a gold surface.1932-620310.1371/journal.pone.0020925https://doaj.org/article/1f9276bfc09842bba7f5d5e2ae6780622011-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/21687744/?tool=EBIhttps://doaj.org/toc/1932-6203The adsorption of proteins on inorganic surfaces is of fundamental biological importance. Further, biomedical and nanotechnological applications increasingly use interfaces between inorganic material and polypeptides. Yet, the underlying adsorption mechanism of polypeptides on surfaces is not well understood and experimentally difficult to analyze. Therefore, we investigate here the interactions of polypeptides with a gold(111) surface using computational molecular dynamics (MD) simulations with a polarizable gold model in explicit water. Our focus in this paper is the investigation of the interaction of polypeptides with β-sheet folds. First, we concentrate on a β-sheet forming model peptide. Second, we investigate the interactions of two domains with high β-sheet content of the biologically important extracellular matrix protein fibronectin (FN). We find that adsorption occurs in a stepwise mechanism both for the model peptide and the protein. The positively charged amino acid Arg facilitates the initial contact formation between protein and gold surface. Our results suggest that an effective gold-binding surface patch is overall uncharged, but contains Arg for contact initiation. The polypeptides do not unfold on the gold surface within the simulation time. However, for the two FN domains, the relative domain-domain orientation changes. The observation of a very fast and strong adsorption indicates that in a biological matrix, no bare gold surfaces will be present. Hence, the bioactivity of gold surfaces (like bare gold nanoparticles) will critically depend on the history of particle administration and the proteins present during initial contact between gold and biological material. Further, gold particles may act as seeds for protein aggregation. Structural re-organization and protein aggregation are potentially of immunological importance.Martin HoeflingSusanna MontiStefano CorniKay Eberhard GottschalkPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 6, Iss 6, p e20925 (2011)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Martin Hoefling Susanna Monti Stefano Corni Kay Eberhard Gottschalk Interaction of β-sheet folds with a gold surface.
description	The adsorption of proteins on inorganic surfaces is of fundamental biological importance. Further, biomedical and nanotechnological applications increasingly use interfaces between inorganic material and polypeptides. Yet, the underlying adsorption mechanism of polypeptides on surfaces is not well understood and experimentally difficult to analyze. Therefore, we investigate here the interactions of polypeptides with a gold(111) surface using computational molecular dynamics (MD) simulations with a polarizable gold model in explicit water. Our focus in this paper is the investigation of the interaction of polypeptides with β-sheet folds. First, we concentrate on a β-sheet forming model peptide. Second, we investigate the interactions of two domains with high β-sheet content of the biologically important extracellular matrix protein fibronectin (FN). We find that adsorption occurs in a stepwise mechanism both for the model peptide and the protein. The positively charged amino acid Arg facilitates the initial contact formation between protein and gold surface. Our results suggest that an effective gold-binding surface patch is overall uncharged, but contains Arg for contact initiation. The polypeptides do not unfold on the gold surface within the simulation time. However, for the two FN domains, the relative domain-domain orientation changes. The observation of a very fast and strong adsorption indicates that in a biological matrix, no bare gold surfaces will be present. Hence, the bioactivity of gold surfaces (like bare gold nanoparticles) will critically depend on the history of particle administration and the proteins present during initial contact between gold and biological material. Further, gold particles may act as seeds for protein aggregation. Structural re-organization and protein aggregation are potentially of immunological importance.
format	article
author	Martin Hoefling Susanna Monti Stefano Corni Kay Eberhard Gottschalk
author_facet	Martin Hoefling Susanna Monti Stefano Corni Kay Eberhard Gottschalk
author_sort	Martin Hoefling
title	Interaction of β-sheet folds with a gold surface.
title_short	Interaction of β-sheet folds with a gold surface.
title_full	Interaction of β-sheet folds with a gold surface.
title_fullStr	Interaction of β-sheet folds with a gold surface.
title_full_unstemmed	Interaction of β-sheet folds with a gold surface.
title_sort	interaction of β-sheet folds with a gold surface.
publisher	Public Library of Science (PLoS)
publishDate	2011
url	https://doaj.org/article/1f9276bfc09842bba7f5d5e2ae678062
work_keys_str_mv	AT martinhoefling interactionofbsheetfoldswithagoldsurface AT susannamonti interactionofbsheetfoldswithagoldsurface AT stefanocorni interactionofbsheetfoldswithagoldsurface AT kayeberhardgottschalk interactionofbsheetfoldswithagoldsurface
_version_	1718424277250736128

Interaction of β-sheet folds with a gold surface.

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