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Related Experiment Video

Updated: Jul 13, 2025

Synthesis and Characterization of 1,2-Dithiolane Modified Self-Assembling Peptides

Synthesis and Characterization of 1,2-Dithiolane Modified Self-Assembling Peptides

Published on: August 20, 2018

Metal-Promoted Higher-Order Assembly of Disulfide-Stapled Helical Barrels.

Ashutosh Agrahari¹, Mark Lipton¹, Jean Chmielewski¹

¹Department of Chemistry, Purdue University, 560 Oval Drive, West Lafayette, IN 47907, USA.

Nanomaterials (Basel, Switzerland)

|October 14, 2023

Summary

Researchers created peptide-based helical barrels that self-assemble into 3D matrices. These biomaterials can host cargo, showing potential for biotechnology applications in cell and tissue growth.

Keywords:

3D matrix amphiphilic peptide biomaterial cargo helical barrel higher order assembly

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Self-Assembly of Gamma-Modified Peptide Nucleic Acids into Complex Nanostructures in Organic Solvent Mixtures

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Last Updated: Jul 13, 2025

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Published on: August 20, 2018

Constructing Thioether/Vinyl Sulfide-tethered Helical Peptides Via Photo-induced Thiol-ene/yne Hydrothiolation

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Published on: August 1, 2018

Self-Assembly of Gamma-Modified Peptide Nucleic Acids into Complex Nanostructures in Organic Solvent Mixtures

Self-Assembly of Gamma-Modified Peptide Nucleic Acids into Complex Nanostructures in Organic Solvent Mixtures

Published on: June 26, 2020

Area of Science:

Biomaterials Science
Supramolecular Chemistry
Protein Engineering

Background:

Peptide-based helical barrels offer a hydrophobic cavity for cargo hosting.
Hierarchical assembly is key for advanced biomaterial design.

Purpose of the Study:

To synthesize disulfide-stapled helical barrels with metal ion ligands.
To investigate the self-assembly of these barrels into higher-order structures.
To explore the potential of these peptide biomaterials in biotechnology.

Main Methods:

Synthesis of disulfide-stapled helical barrels from amphiphilic peptides.
In silico structural optimization of the pentameric helical barrel (5HB1).
Metal-ion-promoted self-assembly into 3D matrices.
Decoration of the matrix with hydrophobic dyes and His-tagged proteins.

Main Results:

A single-step reaction yielded a stable pentameric helical barrel (5HB1) from 16-amino-acid peptides.
In silico analysis revealed a ~6 Å hydrophobic cavity within the 5HB1 structure.
Metal-ion-mediated assembly formed a 3D matrix with tunable decoration capabilities.
The matrix successfully incorporated hydrophobic dyes and His-tagged proteins.

Conclusions:

Disulfide-stapled helical barrels serve as versatile building blocks for hierarchical assembly.
The resulting 3D peptide matrices can encapsulate various molecules and proteins.
This peptide-based biomaterial demonstrates significant potential for biotechnology, including controlled release applications for cell and tissue growth.