Abstract
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.
Highlights
The interactions between proteins and nanoparticles were widely studied in the last decades, and from this emerged numerous open questions and applications in different research areas [1,2,3].For instance, understanding the relationship between the structure and activity of a protein adsorbed on nanoparticles is essential to designing catalyst materials or sensors [4,5,6]
We aim to demonstrate that nanopores can be efficient to determine the volume of the protein corona even if AuNP aggregates are present in the mixture
Our work aimed to investigate the formation of the protein corona under salt condition when both single protein-AuNP and aggregates co-exist in the solution
Summary
The interactions between proteins and nanoparticles were widely studied in the last decades, and from this emerged numerous open questions and applications in different research areas [1,2,3]. Understanding the relationship between the structure and activity of a protein adsorbed on nanoparticles is essential to designing catalyst materials or sensors [4,5,6]. The protein corona can be characterized by different techniques. Circular dichroism gives information about the protein structure. FCS is more sensitive to small particles than DLS, but it requires protein labelling with fluorescent dye. DLS is a label-free technique, but information on single molecules/particles can be difficult to extract when aggregates are present in the mixture
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