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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...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2019
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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. |
format | Online Article Text |
id | pubmed-6862098 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
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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