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Related Experiment Video

Updated: Jan 26, 2026

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Twisted Ribbon Aggregates in a Model Peptide System.

Axel Rüter1, Stefan Kuczera1, Darrin J Pochan2

  • 1Division of Physical Chemistry , Lund University , SE-22100 Lund , Sweden.

Langmuir : the ACS Journal of Surfaces and Colloids
|April 9, 2019
PubMed
Summary

Model peptides self-assemble into ribbon-like structures. These peptide aggregates exhibit a consistent cross-section and twist, explained by a model considering interfacial and stretching energies.

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Area of Science:

  • Supramolecular chemistry
  • Biomaterials science
  • Peptide self-assembly

Background:

  • Peptide self-assembly is a key process in biomaterials.
  • Understanding the structural formation of peptide aggregates is crucial for designing new materials.

Purpose of the Study:

  • To investigate the self-assembly of model peptides A8K and A10K into ribbon-like aggregates.
  • To analyze the structural characteristics and formation mechanism of these peptide ribbons.

Main Methods:

  • High-contrast transmission electron microscopy (TEM) for structural analysis.
  • Development of a theoretical model to explain self-assembly.

Main Results:

  • Peptides A8K and A10K form ~100 nm long, ribbon-like aggregates in water.
  • Aggregates show a constant elliptical cross-section (4x8 nm) and a twist pitch of ~15 nm.
  • The cross-section is independent of peptide concentration.

Conclusions:

  • A model incorporating interfacial and stretching free energies explains the observed ribbon formation and dimensions.
  • The model predicts an optimal number of laminated sheets (N≈15) consistent with experimental findings.