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Researchers developed simple peptide coacervates that form compartments for early cell research. These peptide droplets can encapsulate nucleic acids and catalyze reactions, offering a new path toward synthetic protocells.

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Area of Science:

  • Biochemistry
  • Origin of Life Studies
  • Synthetic Biology

Background:

  • Membraneless compartments in cells form via liquid-liquid phase separation of disordered proteins.
  • Coacervates, similar structures, may have been crucial in early cell formation.
  • Designing simple peptide coacervates for self-assembly has been challenging.

Purpose of the Study:

  • To create a simple peptide-based synthon for self-coacervation.
  • To explore the potential of these peptide coacervates as protocells.
  • To establish design principles for peptide coacervate formation.

Main Methods:

  • Synthesized short peptide synthons with dipeptide stickers and hydrophilic spacers.
  • Investigated self-coacervation behavior and droplet properties (size, water content).
  • Developed redox-responsive disulfide-linked peptide derivatives for reversible compartmentalization.

Main Results:

  • Achieved self-coacervation of peptide synthons into micron-sized droplets at sub-millimolar concentrations.
  • Demonstrated droplets retain significant water content (up to 75 wt%).
  • Showcased reversible compartmentalization, nucleic acid sequestration, and catalytic activity in microreactors.

Conclusions:

  • The designed peptide synthons offer a generalizable route to self-coacervating systems.
  • Redox-responsive peptide coacervates show promise as tunable protocell models.
  • These findings represent a significant step towards creating single-peptide-species coacervate-based protocells.