Monodisperse self-assembly in a model with protein-like interactions

Area of Science:

• Biophysics
• Computational Chemistry
• Materials Science

Background:

• Self-assembly of protein complexes, like viral capsids, is crucial in biology.
• Understanding the principles governing protein assembly can inform the design of novel nanomaterials.
• Patchy particle models offer a simplified yet powerful approach to study complex self-assembly phenomena.

Purpose of the Study:

• To investigate the self-assembly behavior of patchy particles with proteinlike interactions.
• To establish a minimal model for viral capsid and shell-like protein complex assembly.
• To explore the thermodynamics and dynamics of self-assembly across various model parameters.

Main Methods:

• Utilized a minimal model of patchy particles with tunable proteinlike interactions.
• Performed extensive simulations to explore the thermodynamics and dynamics of self-assembly.
• Computed free energy landscapes to analyze the assembly pathways and identify kinetic traps.

Main Results:

• Demonstrated robust assembly of target shell structures across a range of parameters.
• Identified an optimal parameter region where a free energy barrier regulates nucleation.
• Observed that specific interactions prevent malformed shells while maintaining kinetic accessibility.
• Free energy landscapes revealed a funnel-like topography guiding assembly and preventing disordered aggregates.

Conclusions:

• The studied proteinlike interactions provide a robust model for viral capsid assembly.
• A critical free energy barrier is essential for efficient and accurate self-assembly.
• The model successfully balances specificity and kinetic accessibility for forming complete, ordered structures.