Isothermal titration calorimetry as a complementary method for investigating nanoparticle-protein interactions

Area of Science:

• Biomaterials Science
• Nanotechnology
• Biophysics

Background:

• Protein corona formation on nanomaterials in biological media significantly alters their surface properties and behavior.
• Understanding nanoparticle-protein interactions is crucial for predicting nanomaterial fate and function in vivo.
• Isothermal titration calorimetry (ITC) offers a powerful method to study these interactions.

Purpose of the Study:

• To review and synthesize findings from Isothermal Titration Calorimetry (ITC) studies on protein adsorption to various nanomaterials.
• To elucidate the thermodynamic parameters governing nanoparticle-protein interactions.
• To establish relationships between nanomaterial properties and their protein corona characteristics.

Main Methods:

• Review of existing Isothermal Titration Calorimetry (ITC) data on nanomaterial-protein interactions.
• Analysis of thermodynamic parameters including binding affinity (K_a), enthalpy (ΔH), entropy (ΔS), and stoichiometry (n).
• Correlation of nanomaterial surface properties (hydrophilicity, charge, stabilization) with observed protein interactions.

Main Results:

• ITC provides quantitative thermodynamic data (K_a, ΔH, ΔS, n) on in situ protein-nanomaterial binding.
• Nanomaterials with hydrophilic, uncharged surfaces and steric stabilization exhibit the weakest interactions with proteins.
• These specific nanomaterial characteristics lead to minimal non-specific protein adsorption.

Conclusions:

• Isothermal titration calorimetry (ITC) is a valuable complementary technique for mechanistic understanding of the protein corona.
• Engineering nanomaterial surface properties, particularly hydrophilicity and charge, can minimize unwanted protein interactions.
• Minimally interacting nanomaterials hold promise for controlled protein corona engineering.