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Revealing the Nanoparticle-Protein Corona with a Solid-State Nanopore

Protein adsorption at the liquid–solid interface is an old but not totally solved topic. One challenge is to find an easy way to characterize the protein behavior on nanoparticles and make a correlation with its intrinsic properties. This work aims to investigate protein adsorption on gold nanoparti...

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Detalles Bibliográficos
Autores principales: Coglitore, Diego, Coulon, Pierre Eugene, Janot, Jean-Marc, Balme, Sébastien
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6862098/
https://www.ncbi.nlm.nih.gov/pubmed/31661780
http://dx.doi.org/10.3390/ma12213524
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author Coglitore, Diego
Coulon, Pierre Eugene
Janot, Jean-Marc
Balme, Sébastien
author_facet Coglitore, Diego
Coulon, Pierre Eugene
Janot, Jean-Marc
Balme, Sébastien
author_sort Coglitore, Diego
collection PubMed
description Protein adsorption at the liquid–solid interface is an old but not totally solved topic. One challenge is to find an easy way to characterize the protein behavior on nanoparticles and make a correlation with its intrinsic properties. This work aims to investigate protein adsorption on gold nanoparticles and the colloidal properties. The protein panel was chosen from different structural categories (mainly-α, mainly-β or mix-αβ). The result shows that the colloidal stability with salt addition does not depend on the structural category. Conversely, using the single nanopore technique, we show that the mainly-α proteins form a smaller corona than the mainly-β proteins. We assign these observations to the lower internal energy of α-helices, making them more prone to form a homogeneous corona layer.
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spelling pubmed-68620982019-12-05 Revealing the Nanoparticle-Protein Corona with a Solid-State Nanopore Coglitore, Diego Coulon, Pierre Eugene Janot, Jean-Marc Balme, Sébastien Materials (Basel) Article Protein adsorption at the liquid–solid interface is an old but not totally solved topic. One challenge is to find an easy way to characterize the protein behavior on nanoparticles and make a correlation with its intrinsic properties. This work aims to investigate protein adsorption on gold nanoparticles and the colloidal properties. The protein panel was chosen from different structural categories (mainly-α, mainly-β or mix-αβ). The result shows that the colloidal stability with salt addition does not depend on the structural category. Conversely, using the single nanopore technique, we show that the mainly-α proteins form a smaller corona than the mainly-β proteins. We assign these observations to the lower internal energy of α-helices, making them more prone to form a homogeneous corona layer. MDPI 2019-10-28 /pmc/articles/PMC6862098/ /pubmed/31661780 http://dx.doi.org/10.3390/ma12213524 Text en © 2019 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Coglitore, Diego
Coulon, Pierre Eugene
Janot, Jean-Marc
Balme, Sébastien
Revealing the Nanoparticle-Protein Corona with a Solid-State Nanopore
title Revealing the Nanoparticle-Protein Corona with a Solid-State Nanopore
title_full Revealing the Nanoparticle-Protein Corona with a Solid-State Nanopore
title_fullStr Revealing the Nanoparticle-Protein Corona with a Solid-State Nanopore
title_full_unstemmed Revealing the Nanoparticle-Protein Corona with a Solid-State Nanopore
title_short Revealing the Nanoparticle-Protein Corona with a Solid-State Nanopore
title_sort revealing the nanoparticle-protein corona with a solid-state nanopore
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6862098/
https://www.ncbi.nlm.nih.gov/pubmed/31661780
http://dx.doi.org/10.3390/ma12213524
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