Thermal Compaction of Disordered and Elastin-like Polypeptides: A Temperature-Dependent, Sequence-Specific...

Area of Science:

• Biomaterials Science
• Computational Biology
• Polymer Chemistry

Background:

• Elastin-like polypeptides (ELPs) exhibit temperature-dependent solubility transitions.
• These transitions are crucial for ELP applications but are sensitive to sequence and concentration.
• Predicting these transitions accurately is vital for material design.

Purpose of the Study:

• To develop a sequence-specific coarse-grained (CG) simulation model for ELPs.
• To accurately reproduce the temperature-dependent solubility transitions (cloud points) of ELPs.
• To enable efficient simulation of large-scale ELP structures.

Main Methods:

• Developed a temperature-dependent, implicit solvent, sequence-specific CG simulation model.
• Built upon the self-organized polymer model for intrinsically disordered polypeptides (SOP-IDP).
• Incorporated a semi-empirical function for temperature-dependent hydrophobic interactions.

Main Results:

• The model accurately reproduces transition temperatures for various ELPs based on sequence length and guest residue identity.
• Successfully captured thermal compactions in hydrophobic intrinsically disordered polypeptides (IDPs).
• Demonstrated high computational efficiency characteristic of CG models.

Conclusions:

• The developed CG model provides accurate predictions of ELP phase behavior.
• The model is suitable for simulating complex ELP systems like networks and hydrogels.
• This work advances the computational design of ELP-based materials.