Thermodynamics and models for small nanoparticles upon protein adsorption

Area of Science:

• Nanotechnology and Materials Science
• Biochemistry and Molecular Biology
• Surface Chemistry

Background:

• The protein corona forms when proteins adsorb onto larger nanoparticles (10-100s of nm) in biological systems.
• Small nanoparticles (<10 nm), such as quantum dots and nanoclusters, are comparable in size to proteins.
• The formation of protein adsorption layers on small nanoparticles remains less understood compared to larger counterparts.

Purpose of the Study:

• To investigate whether proteins can adsorb onto the surface of small nanoparticles.
• To explore the detailed interactions, characterization methods, and thermodynamic mechanisms governing these associations.
• To introduce and emphasize the concept of a 'protein complex' for small nanoparticle-protein interactions.

Main Methods:

• Review and summarization of existing characterization techniques for nanoparticle-protein interactions.
• Analysis of thermodynamic principles governing protein adsorption onto small nanomaterials.
• Discussion of various interaction models applicable to small nanoparticle-protein systems.

Main Results:

• Proteins can indeed adsorb onto small nanoparticles, forming distinct structures.
• The interactions are governed by specific thermodynamic mechanisms and can be characterized by established methods.
• A new conceptual framework, the 'protein complex', is proposed to describe these interactions more accurately than the traditional 'protein corona'.

Conclusions:

• Small nanoparticles interact with proteins, forming structures that differ from the conventional protein corona.
• The concept of a 'protein complex' provides a more fitting description for protein adsorption on sub-10 nm nanomaterials.
• Understanding these interactions is crucial for the safe and effective application of small nanomaterials in biological systems.