Design Rules for the Sequestration of Viruses into Polypeptide Complex Coacervates.

Area of Science:

• Biophysics
• Materials Science
• Biotechnology

Background:

• Encapsulation enhances protein and virus stability and delivery.
• Complex coacervation, a liquid-liquid phase separation of oppositely charged polymers, is a promising encapsulation method.

Purpose of the Study:

• Investigate virus encapsulation using polypeptide-based coacervates.
• Determine how peptide chemistry, chain length, charge patterning, and hydrophobicity affect virus incorporation.
• Characterize the influence of virus charge, hydrophobicity, and surface chemistry on encapsulation efficiency.

Main Methods:

• Utilized polypeptide-based coacervates for encapsulation.
• Employed two nonenveloped viruses: porcine parvovirus (PPV) and human rhinovirus (HRV).
• Compared virus encapsulation based on varying polypeptide properties and virus characteristics.

Main Results:

• Electrostatic interactions (net charge) between viruses and polypeptides are primary drivers of encapsulation.
• Virus hydrophobicity influences the enhancement of uptake with increased peptide hydrophobicity.
• Charge patterning and polypeptide chain length exhibit nonintuitive effects on the range of coacervate compositions for virus incorporation.

Conclusions:

• Virus encapsulation in coacervates is governed by electrostatic forces and virus hydrophobicity.
• Polypeptide sequence and structure critically control virus uptake into coacervates.
• Findings provide biophysical insights for developing advanced formulation strategies for proteins and viruses.