Coarse-Grained Simulation of Protein-Imprinted Hydrogels.

Area of Science:

• Polymer Chemistry
• Computational Chemistry
• Biomaterials Science

Background:

• Protein-imprinted polymers (PIPs) are crucial for molecular recognition and separation.
• Simulating PIPs requires accurate force fields and robust simulation methods.
• Understanding protein-polymer interactions is key to designing effective imprinted materials.

Purpose of the Study:

• To adapt the MARTINI force field for acrylic functional monomers in PIP simulations.
• To investigate the complexation, cross-linking, washing, and rebinding processes of proteins within PIPs.
• To compare the performance of two different gel formulations for protein imprinting.

Main Methods:

• Utilized a globally controlled grand canonical Monte Carlo (GCMC) simulation combined with molecular dynamics (MD).
• Adapted the MARTINI force field for acrylic functional monomers.
• Simulated two gel formulations: one with polar monomers and another with additional charged monomers.
• Evaluated imprinted hydrogels using lysozyme and cytochrome c proteins.

Main Results:

• The adapted MARTINI force field successfully simulated PIPs, including various process steps.
• GCMC-MD simulations achieved proper hydration and swelling of the imprinted hydrogels.
• Analysis revealed distinct diffusion mechanisms and interactions for lysozyme and cytochrome c within the gels.
• Differences in protein-monomer interactions significantly affected specific and nonspecific binding.

Conclusions:

• The adapted MARTINI force field is suitable for simulating protein-imprinted acrylic polymers.
• Gel formulation and protein properties critically influence imprinting efficiency and protein diffusion.
• Molecular simulations provide valuable insights into the complex interactions governing PIP performance.