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Modelling network formation in folded protein hydrogels by cluster aggregation kinetics.

Kalila R Cook1, David Head2, Lorna Dougan1,3

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This study introduces a kinetic model for protein hydrogel formation, simplifying complex protein behavior. The model predicts network structure and porosity, offering insights into diffusion-limited to reaction-limited cluster aggregation mechanisms.

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Area of Science:

  • Materials Science
  • Biomaterials Engineering
  • Polymer Chemistry

Background:

  • Protein-based hydrogels offer unique biological functionality and responsiveness.
  • Modeling folded proteins as colloids simplifies network formation studies.
  • Computationally intensive simulations of protein complexity can be avoided.

Purpose of the Study:

  • To present a kinetic lattice-based model for simulating folded protein-based hydrogel formation.
  • To identify gel percolation critical points and explore network formation mechanisms.
  • To predict final network structure, fractal dimensions, and gel porosity.

Main Methods:

  • Developed a kinetic lattice-based model for irreversible chemical crosslinking.
  • Simulated network formation across diffusion-limited cluster aggregation (DLCA) and reaction-limited cluster aggregation (RLCA) regimes.
  • Analyzed pore size distribution and fractal dimensions of the resulting networks.

Main Results:

  • Identified a crossover between DLCA and RLCA mechanisms based on protein volume fraction.
  • Demonstrated that final network structure is dictated by the percolation point structure.
  • Observed larger maximal pores in RLCA gels compared to DLCA gels at studied volume fractions.

Conclusions:

  • The kinetic model accurately predicts protein hydrogel network structure and porosity.
  • The model provides insights into the relationship between aggregation mechanisms and material properties.
  • Results align with experimental observations and offer a tool for designing protein hydrogels.