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Sequence-encoded phase behavior and functionality of short peptide coacervates.

Jiahua Wang1, Manzar Abbas2, Yuening Qiu3

  • 1Department of Radiology, Shanghai Jiao Tong University School of Medicine Affiliated Sixth People's Hospital, Shanghai 200233, China.

Journal of Colloid and Interface Science
|December 9, 2025
PubMed
Summary
This summary is machine-generated.

Researchers designed simple peptide coacervates using liquid-liquid phase separation (LLPS). These peptide coacervates show tunable phase behavior and can encapsulate biomolecules, offering potential for protocells and drug delivery.

Keywords:
Catalytic compartmentsDelivery vehicleLiquid-liquid phase separationPeptidesSimple Coacervates

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Area of Science:

  • Biochemistry
  • Materials Science
  • Origin of Life Studies

Background:

  • Membraneless cellular compartments, formed by liquid-liquid phase separation (LLPS) of intrinsically disordered proteins, are crucial for cellular organization.
  • Short peptide coacervates, also formed via LLPS, are hypothesized to be primitive cellular compartments relevant to early life.
  • The molecular principles governing peptide-based LLPS are not well understood.

Purpose of the Study:

  • To investigate the molecular grammar dictating the phase behavior of short peptide coacervates.
  • To establish a predictive framework for designing peptide-based coacervates.
  • To explore the functional potential of these coacervates as protocell models and for intracellular delivery.

Main Methods:

  • Systematic investigation of phase separation in oxidized dimeric forms of short cysteine-terminated peptides acting as "sticker" units.
  • Analysis of the correlation between peptide sequence (arginine to aromatic ratio, aromatic residue identity) and phase behavior (saturation concentration).
  • Incorporation of an enzyme-inspired catalytic triad (Ser-His-Asp) and redox-active disulfide spacers to impart catalytic activity and responsive behavior.

Main Results:

  • LLPS behavior is primarily governed by the arginine to aromatic residue ratio and the identity of the aromatic residue (Phe, Tyr, Trp).
  • Saturation concentration (Csat) linearly correlates with aromatic residue hydrophobicity, with increased hydrophobicity enhancing phase separation.
  • Peptide coacervates demonstrated catalytic activity and reversible condensation/dissolution in response to glutathione, enabling cargo (mRNA) delivery.

Conclusions:

  • A minimal, predictive framework for designing peptide-based coacervates based on Rarg/aro and aromatic residue identity was established.
  • Functional peptide coacervates can be engineered for applications in intracellular delivery, mRNA vaccines, and understanding the origins of life.
  • Responsive peptide coacervates offer a versatile platform for controlled release of biomolecular cargos.