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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Published inMaterials Vol. 12; no. 21; p. 3524
Main Authors Coglitore, Diego, Coulon, Pierre Eugene, Janot, Jean-Marc, Balme, Sébastien
Format Journal Article
LanguageEnglish
Published Basel MDPI AG 01.11.2019
MDPI
Subjects
Chemical Sciences
Experiments
Glucose
Helices
Internal energy
Liquid-solid interfaces
Nanoparticles
nanopore
Protein adsorption
protein corona
Proteins
Receivers & amplifiers
Silicon nitride
single molecule
Software
Spectrum analysis
France
United States > US
Germany
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Summary: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.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
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content type line 23
ISSN:1996-1944
1996-1944
DOI:10.3390/ma12213524