Role of Charge Patterning and Hydrophobicity in Peptide-Based Complex Coacervates

Area of Science:

• Biophysics
• Materials Science
• Protein Chemistry

Background:

• Complex coacervation is a key model for understanding intrinsically disordered proteins (IDPs) in cellular condensates.
• Controlling the self-assembly and material properties of biological condensates is crucial for cellular function.

Purpose of the Study:

• To investigate the impact of charge patterning and hydrophobicity on the phase behavior and rheology of peptide-based coacervates.
• To explore sequence-controlled materials as a platform for engineering tunable self-assembling systems.

Main Methods:

• Characterization of phase behavior and rheology of coacervates formed from peptides with regular repeating sequences.
• Systematic variation of peptide sequence to analyze effects of charged block size and hydrophobic segment incorporation.

Main Results:

• Increasing charged block size enhances salt resistance through electrostatic cooperativity.
• Incorporating small hydrophobic segments stabilizes coacervates and increases viscosity via hydrophobic clustering.
• Peptide structural conformations in shorter block sizes may also contribute to increased coacervate viscosity.

Conclusions:

• Sequence-controlled peptides provide a versatile platform for designing self-assembling materials.
• Tunable phase and mechanical properties of coacervates can be achieved by controlling peptide sequence.
• Findings advance the understanding of coacervation principles for biomaterials engineering.