Structural determinants for protein adsorption/non-adsorption to silica surface.

Structural determinants for protein adsorption/non-adsorption to silica surface.

The understanding of the mechanisms involved in the interaction of proteins with inorganic surfaces is of major interest in both fundamental research and applications such as nanotechnology. However, despite intense research, the mechanisms and the structural determinants of protein/surface interact...

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Autores principales: Christelle Mathé, Stéphanie Devineau, Jean-Christophe Aude, Gilles Lagniel, Stéphane Chédin, Véronique Legros, Marie-Hélène Mathon, Jean-Philippe Renault, Serge Pin, Yves Boulard, Jean Labarre
Formato: article
Lenguaje:EN
Publicado: Public Library of Science (PLoS) 2013
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Medicine
R
Science
Q
Acceso en línea:https://doaj.org/article/8f3622dcb0be43119f7ac2094d8624cf
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spelling oai:doaj.org-article:8f3622dcb0be43119f7ac2094d8624cf2021-11-18T08:44:49ZStructural determinants for protein adsorption/non-adsorption to silica surface.1932-620310.1371/journal.pone.0081346https://doaj.org/article/8f3622dcb0be43119f7ac2094d8624cf2013-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/24282583/?tool=EBIhttps://doaj.org/toc/1932-6203The understanding of the mechanisms involved in the interaction of proteins with inorganic surfaces is of major interest in both fundamental research and applications such as nanotechnology. However, despite intense research, the mechanisms and the structural determinants of protein/surface interactions are still unclear. We developed a strategy consisting in identifying, in a mixture of hundreds of soluble proteins, those proteins that are adsorbed on the surface and those that are not. If the two protein subsets are large enough, their statistical comparative analysis must reveal the physicochemical determinants relevant for adsorption versus non-adsorption. This methodology was tested with silica nanoparticles. We found that the adsorbed proteins contain a higher number of charged amino acids, particularly arginine, which is consistent with involvement of this basic amino acid in electrostatic interactions with silica. The analysis also identified a marked bias toward low aromatic amino acid content (phenylalanine, tryptophan, tyrosine and histidine) in adsorbed proteins. Structural analyses and molecular dynamics simulations of proteins from the two groups indicate that non-adsorbed proteins have twice as many π-π interactions and higher structural rigidity. The data are consistent with the notion that adsorption is correlated with the flexibility of the protein and with its ability to spread on the surface. Our findings led us to propose a refined model of protein adsorption.Christelle MathéStéphanie DevineauJean-Christophe AudeGilles LagnielStéphane ChédinVéronique LegrosMarie-Hélène MathonJean-Philippe RenaultSerge PinYves BoulardJean LabarrePublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 8, Iss 11, p e81346 (2013)
institution DOAJ
collection DOAJ
language EN
topic Medicine
R
Science
Q
spellingShingle Medicine
R
Science
Q
Christelle Mathé
Stéphanie Devineau
Jean-Christophe Aude
Gilles Lagniel
Stéphane Chédin
Véronique Legros
Marie-Hélène Mathon
Jean-Philippe Renault
Serge Pin
Yves Boulard
Jean Labarre
Structural determinants for protein adsorption/non-adsorption to silica surface.
description The understanding of the mechanisms involved in the interaction of proteins with inorganic surfaces is of major interest in both fundamental research and applications such as nanotechnology. However, despite intense research, the mechanisms and the structural determinants of protein/surface interactions are still unclear. We developed a strategy consisting in identifying, in a mixture of hundreds of soluble proteins, those proteins that are adsorbed on the surface and those that are not. If the two protein subsets are large enough, their statistical comparative analysis must reveal the physicochemical determinants relevant for adsorption versus non-adsorption. This methodology was tested with silica nanoparticles. We found that the adsorbed proteins contain a higher number of charged amino acids, particularly arginine, which is consistent with involvement of this basic amino acid in electrostatic interactions with silica. The analysis also identified a marked bias toward low aromatic amino acid content (phenylalanine, tryptophan, tyrosine and histidine) in adsorbed proteins. Structural analyses and molecular dynamics simulations of proteins from the two groups indicate that non-adsorbed proteins have twice as many π-π interactions and higher structural rigidity. The data are consistent with the notion that adsorption is correlated with the flexibility of the protein and with its ability to spread on the surface. Our findings led us to propose a refined model of protein adsorption.
format article
author Christelle Mathé
Stéphanie Devineau
Jean-Christophe Aude
Gilles Lagniel
Stéphane Chédin
Véronique Legros
Marie-Hélène Mathon
Jean-Philippe Renault
Serge Pin
Yves Boulard
Jean Labarre
author_facet Christelle Mathé
Stéphanie Devineau
Jean-Christophe Aude
Gilles Lagniel
Stéphane Chédin
Véronique Legros
Marie-Hélène Mathon
Jean-Philippe Renault
Serge Pin
Yves Boulard
Jean Labarre
author_sort Christelle Mathé
title Structural determinants for protein adsorption/non-adsorption to silica surface.
title_short Structural determinants for protein adsorption/non-adsorption to silica surface.
title_full Structural determinants for protein adsorption/non-adsorption to silica surface.
title_fullStr Structural determinants for protein adsorption/non-adsorption to silica surface.
title_full_unstemmed Structural determinants for protein adsorption/non-adsorption to silica surface.
title_sort structural determinants for protein adsorption/non-adsorption to silica surface.
publisher Public Library of Science (PLoS)
publishDate 2013
url https://doaj.org/article/8f3622dcb0be43119f7ac2094d8624cf
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