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Area of Science:

  • Biophysics
  • Soft Matter Physics
  • Biochemistry

Background:

  • The interface of biomolecular condensates is vital for their function but poorly understood.
  • Polypeptides with charged, polar, and aromatic residues form these condensates in aqueous solutions.

Purpose of the Study:

  • Investigate the interfacial structure of polypeptide condensates.
  • Explore the interplay between electrostatic and nonelectrostatic interactions.
  • Determine how parameters like charge fraction, aromatic fraction, interaction strength, and salt concentration influence interfacial organization.

Main Methods:

  • Developed an inhomogeneous mean-field theory.
  • Systematically analyzed the effects of varying charge fraction (α), aromatic fraction (β), specific interaction strength (εs), and salt concentration (ρs).

Main Results:

  • Condensate interfaces exhibit an electric double-layer structure at finite charge fraction.
  • Polypeptide concentration profiles show depletion and overshoot layers in the absence of salt.
  • Increased salt concentration narrows interfacial width and weakens charge separation for condensates stabilized by specific attractions.
  • Electrostatic potential profiles are asymmetric across the interface.

Conclusions:

  • The study provides insights into the regulation of interfacial organization in polypeptide condensates.
  • Predictions align qualitatively with experimental observations.
  • Findings may guide the rational design of biomolecular condensates with specific interfacial properties.