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Related Concept Videos

Protein Folding01:25

Protein Folding

Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
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Updated: Jun 13, 2026

Preparation of Mechanically Stable Self-Assembled Peptides Hydrogels
05:24

Preparation of Mechanically Stable Self-Assembled Peptides Hydrogels

Published on: September 6, 2024

A reductive trigger for peptide self-assembly and hydrogelation.

Charles J Bowerman1, Bradley L Nilsson

  • 1Department of Chemistry, University of Rochester, Rochester, New York 14627-0216, USA.

Journal of the American Chemical Society
|April 22, 2010
PubMed
Summary
This summary is machine-generated.

Researchers developed a novel reductive trigger for peptide self-assembly and hydrogel formation. This method allows controlled formation of rigid hydrogels from self-assembling peptides in response to environmental stimuli.

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Preparation of Mechanically Stable Self-Assembled Peptides Hydrogels
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09:34

Synthesis of Information-bearing Peptoids and their Sequence-directed Dynamic Covalent Self-assembly

Published on: February 6, 2020

Area of Science:

  • Biomaterials Science
  • Supramolecular Chemistry
  • Chemical Engineering

Background:

  • Stimulus-responsive materials offer precise control over self-assembly processes.
  • Peptide self-assembly is a versatile platform for creating functional nanomaterials.
  • Hydrogels are critical in drug delivery, tissue engineering, and soft robotics.

Purpose of the Study:

  • To develop a novel reductive trigger for peptide self-assembly.
  • To engineer a peptide system that undergoes controlled hydrogelation.
  • To investigate the mechanism of stimulus-induced peptide self-assembly and hydrogel formation.

Main Methods:

  • Design and synthesis of a cyclized peptide sequence (Ac-C(FKFE)(2)CG-NH(2)).
  • Disulfide bond formation to create a macrocyclic peptide structure.
  • Reductive cleavage of the disulfide bond to trigger peptide conformational change and self-assembly.

Main Results:

  • The macrocyclic peptide was conformationally restrained, preventing beta-sheet formation.
  • Disulfide bond reduction released the conformational restraint, inducing rapid beta-sheet adoption.
  • Self-assembly led to fibrillar superstructures and the formation of rigid, viscoelastic hydrogels at sufficient concentrations.

Conclusions:

  • A novel reductive trigger effectively controls peptide self-assembly and hydrogelation.
  • The developed system demonstrates stimulus-responsive behavior for material design.
  • This approach enables the creation of tunable hydrogels for advanced applications.