Electrostatically-controlled protein adsorption onto lipid bilayer: modeling adsorbate aggregation behavior

Area of Science:

• Biophysical Chemistry
• Surface Science
• Computational Modeling

Background:

• Protein adsorption to surfaces is crucial in biological and industrial applications.
• Understanding protein aggregation and its impact on adsorption is essential for controlling surface interactions.

Purpose of the Study:

• To simulate and analyze electrostatically-controlled protein adsorption onto membrane surfaces.
• To identify hallmarks of protein oligomerization and self-association during adsorption.
• To provide guidance for designing experiments to detect protein self-association.

Main Methods:

• Utilized adsorption models based on scaled particle theory (SPT) and double layer theories.
• Simulated protein adsorption for both non-associating and self-associating ligands.
• Calculated binding isotherms for monomeric and oligomeric protein species under varying conditions.

Main Results:

• Protein adsorption behavior, particularly for monomers, is highly sensitive to protein aggregation state.
• Key indicators for identifying protein oligomerization were determined.
• The influence of parameters like concentration, charge, pH, and ionic strength on adsorption was analyzed.

Conclusions:

• Protein self-association significantly alters adsorption characteristics.
• The study provides a framework for distinguishing between monomeric and oligomeric protein adsorption.
• Practical guidelines are offered for optimizing binding experiments to study protein self-association.