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Monitoring Protein Adsorption with Solid-state Nanopores
Published on: December 2, 2011
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Revealing the Nanoparticle-Protein Corona with a Solid-State Nanopore
Diego Coglitore1, Pierre Eugene Coulon2, Jean-Marc Janot3
1Institut Européen des Membranes, UMR5635, Université de Montpellier CNRS ENSCM, Place Eugène Bataillon, 34090 Montpellier, France. diego.coglitore@gmail.com.
Materials (Basel, Switzerland)
|October 31, 2019
Summary
Protein adsorption on gold nanoparticles differs by protein structure. Mainly-alpha proteins form smaller coronas than mainly-beta proteins, impacting nanoparticle behavior and stability.
Area of Science:
- Biophysics
- Materials Science
- Nanotechnology
Background:
- Protein adsorption at liquid-solid interfaces is a complex phenomenon.
- Characterizing protein behavior on nanoparticles and correlating it with intrinsic properties remains challenging.
Purpose of the Study:
- To investigate protein adsorption on gold nanoparticles.
- To correlate protein structure with colloidal properties and corona formation.
Main Methods:
- Utilized a panel of proteins from different structural categories (mainly-alpha, mainly-beta, mix-alpha-beta).
- Assessed colloidal stability with salt addition.
- Employed the single nanopore technique to analyze protein corona characteristics.
Main Results:
- Colloidal stability was independent of protein structural category upon salt addition.
- Mainly-alpha proteins formed significantly smaller coronas compared to mainly-beta proteins.
- Protein structure influences corona layer homogeneity and size.
Conclusions:
- The lower internal energy of alpha-helices promotes a more homogeneous corona layer.
- Protein structure is a key determinant of corona characteristics on nanoparticles.
