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Protein Complex Assembly

Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types. Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...

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Updated: May 30, 2025

Author Spotlight: Improving the Production of Self-Assembling Fibers and Peptide Hydrogels for Superior Biocompatibility

Author Spotlight: Improving the Production of Self-Assembling Fibers and Peptide Hydrogels for Superior Biocompatibility

Published on: September 6, 2024

Peptide-Based Complex Coacervates Stabilized by Cation-π Interactions for Cell Engineering.

Yue Sun¹, Xi Wu¹, Jianguo Li^2,3

¹Center for Sustainable Materials (SusMat), School of Materials Science and Engineering, Nanyang Technological University, Singapore 639798, Singapore.

Journal of the American Chemical Society

|January 26, 2025

Summary

This summary is machine-generated.

Researchers developed peptide coacervates for intracellular delivery. Cation-π interactions enhance coacervate stability and enable tunable cargo release, showing promise for gene editing tools and therapeutics.

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Area of Science:

Biomaterials Science
Molecular Biology
Nanotechnology

Background:

Complex coacervation involves liquid-liquid phase separation of oppositely charged macromolecules.
Peptide-based coacervates are emerging as effective intracellular delivery vehicles for large biomolecules.
Understanding coacervate assembly/disassembly is crucial for optimizing cargo delivery and release kinetics.

Purpose of the Study:

To design and characterize histidine-rich peptides for tunable complex coacervate formation.
To investigate the role of specific amino acid residues and intermolecular interactions in coacervate stability.
To evaluate the potential of these peptide coacervates for intracellular delivery of various macromolecules.

Main Methods:

Systematic incorporation of cationic, anionic, and aromatic residues into peptide sequences.
Modulation of intermolecular interactions, including cation-π interactions, to control coacervation.
Grafting of disulfide-based self-immolative side chains to enhance stability and control release.
In vitro and in cellulo testing for delivery of proteins, mRNA, and CRISPR/Cas9 systems.

Main Results:

Cation-π interactions between arginine and aromatic residues significantly stabilize peptide coacervates.
Coacervate disassembly and cargo release are triggered in protein-rich intracellular environments.
Grafted coacervates demonstrate enhanced stability and efficient delivery of diverse cargo, including mRNA and CRISPR/Cas9.
Successful delivery was achieved in challenging cell types, such as macrophages.

Conclusions:

Peptide-based coacervates offer a versatile platform for intracellular delivery.
Cation-π interactions are key to designing stable and responsive coacervates.
This approach expands the potential of peptide coacervates in biomedicine and biotechnology, particularly for gene editing applications.