A Mechanistic Approach to Modeling Single Protein Adsorption at Solid-Water Interfaces.

Area of Science:

• Biochemistry
• Physical Chemistry
• Molecular Biology

Background:

• Protein adsorption is crucial in various biological and industrial applications.
• Understanding the kinetics and thermodynamics of protein adsorption is complex.
• Bacteriophage T4 lysozyme mutants offer a model system to study protein stability effects on adsorption.

Purpose of the Study:

• To develop a kinetic model for single-component protein adsorption.
• To extend the model for simulating multi-protein solutions.
• To investigate the adsorption behavior of bacteriophage T4 lysozyme mutants with varying structural stability.

Main Methods:

• Developed a kinetic adsorption model with two distinct adsorbed states (binding strengths and occupied areas).
• Incorporated an increasing energy barrier by formulating time-dependent adsorption rate constants.
• Utilized the Marquardt method for numerical analysis and parameter estimation.

Main Results:

• Model parameters were consistent with the influence of structural stability on adsorption.
• Less stable protein variants showed a preference for the more tightly bound, conformationally altered adsorbed state.
• The model successfully simulated adsorption of site-directed mutants of bacteriophage T4 lysozyme.

Conclusions:

• The developed kinetic model accurately predicts protein adsorption behavior based on structural stability.
• The model provides insights into the conformational changes and binding affinities during protein adsorption.
• This approach is extensible to more complex multi-protein adsorption systems.