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Updated: May 28, 2026

Monitoring Protein Adsorption with Solid-state Nanopores
Published on: December 2, 2011
Soft interactions at nanoparticles alter protein function and conformation in a size dependent manner.
Jing Wang1, Uffe B Jensen, Grethe V Jensen
1Interdisciplinary NanoscienceCenter (iNANO), Aarhus University, 7400 Herning, Denmark.
Weak interactions between proteins and nanoparticles alter protein structure and activity. Nanoparticle size critically influences these effects, providing insights into the soft protein corona in biological systems.
Area of Science:
- Biophysics
- Materials Science
- Biochemistry
Background:
- Understanding protein-nanoparticle (NP) interactions is crucial for biological applications.
- The soft protein corona forms via weak, noncovalent interactions in biological fluids.
- Studying these interactions models biological interfaces and nanoparticle behavior.
Purpose of the Study:
- To investigate weak protein-nanoparticle interactions in a low binding regime.
- To model the soft protein corona using Subtilisin Carlsberg (SC) and silica NPs.
- To determine the influence of NP size on protein conformation and enzymatic activity.
Main Methods:
- Centrifugation-based separations to analyze protein-NP binding.
- Small-angle X-ray scattering (SAXS) to probe structural changes.
- Circular dichroism (CD) spectroscopy to assess secondary and tertiary structure.
- Enzyme kinetics assays to measure activity changes.
Main Results:
- Weak, reversible interactions were observed between SC and silica NPs.
- Significant alterations in SC conformation and enzymatic activity were detected.
- These changes were dependent on the nanoparticle size.
- Bovine serum albumin showed strong interactions, serving as a reference.
Conclusions:
- Nanoparticle size plays a critical role in modulating protein structure and function.
- Weak protein-NP interactions can significantly impact enzyme kinetics.
- This study provides a model for understanding the soft protein corona.
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