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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.
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Related Experiment Video

Updated: Jun 24, 2025

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides

Published on: November 21, 2013

Self-Sorting vs Coassembly in Peptide Amphiphile Supramolecular Nanostructures.

M Hussain Sangji¹, Sieun Ruth Lee², Hiroaki Sai³

¹Department of Biomedical Engineering, Northwestern University, 2145 Sheridan Road, Evanston, Illinois 60208, United States.

|June 7, 2024

Summary

Researchers designed peptide amphiphiles (PAs) that either self-sort or coassemble into nanostructures. Opposite chiral PAs self-sorted, while mixed chiral PAs coassembled, offering new biomolecular design possibilities.

Keywords:

correlative imaging peptide amphiphile self-assembly self-sorting nanostructures supramolecular chirality

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Last Updated: Jun 24, 2025

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Published on: April 8, 2020

Area of Science:

Supramolecular Chemistry
Nanotechnology
Materials Science

Background:

Designing multi-component supramolecular nanostructures is key to integrating functions.
Understanding self-sorting and coassembly behaviors is crucial for advanced materials.
Peptide amphiphiles (PAs) are versatile building blocks for self-assembling nanostructures.

Purpose of the Study:

To investigate the self-sorting and coassembly behaviors of three different peptide amphiphiles (PAs).
To understand how supramolecular chirality influences the assembly of binary PA systems.
To explore the design principles for creating functional self-assembling biomolecular materials.

Main Methods:

Utilized atomic force microscopy (AFM) to analyze nanoscale morphology.
Employed confocal laser scanning microscopy (CLSM) to track fluorescently labeled monomers.
Synthesized and characterized three distinct peptide amphiphiles with β-sheet forming capabilities.

Main Results:

Identified binary PA systems that exhibit either self-sorting or coassembly.
Observed that PAs with opposite supramolecular chirality self-sorted into distinct nanostructures.
Found that PAs forming mixed chiral assemblies (right-handed, left-handed, flat) coassembled with other PAs.

Conclusions:

The energy barrier to altering β-sheet twist handedness influences coassembly behavior.
Self-sorting is driven by opposite supramolecular chirality in PA systems.
These findings enable the design of biomolecular nanostructures with dual bioactivity or interpenetrating networks.