Related Experiment Video
Updated: Mar 9, 2026

09:34
Synthesis of Information-bearing Peptoids and their Sequence-directed Dynamic Covalent Self-assembly
Published on: February 6, 2020
8.1K
Optically Controlled Peptide-Based Reconfigurable Folding via Regular Monodisperse Azobenzene Arrangement
Haolong Ye1, Yin Liu1, Tianzi Chen1
1National Engineering Research Center for Biomaterials, College of Biomedical Engineering, Sichuan University, Chengdu 610064, China.
Journal of the American Chemical Society
|March 7, 2026
Summary
Researchers developed novel peptide-based nanosheets (MPANs) that can reconfigure into various 3D shapes using light. This breakthrough overcomes challenges in peptide nanotechnology, enabling controllable nanostructure formation for advanced devices.
Area of Science:
- Supramolecular chemistry
- Nanotechnology
- Materials science
Background:
- Reconfigurable nanostructures offer an alternative to traditional nanotechnology methods.
- Peptide-based supramolecular systems face challenges due to conflicting structural integrity and reconfigurability needs, stemming from poor bond orthogonality.
Purpose of the Study:
- To design a peptide supramolecular system that decouples framework and reconfigurable bonds.
- To create morphologically controllable 3D nanostructures from 2D peptide nanosheets.
Main Methods:
- Utilized homotetrameric peptide coiled-coils to achieve monodisperse arrangement of azobenzene molecules in a 2D plane.
- Developed monolayered peptide-AZO nanosheets (MPANs) with isolated and dispersed reconfigurable azobenzene units.
- Investigated photoinduced reversible multilayer folding of MPANs into 3D structures.
Main Results:
- Successfully created MPANs, a novel peptide supramolecular architecture.
- Achieved photoinduced reversible folding of MPANs into 3D nanostructures.
- Demonstrated tailorable surface chemistries leading to diverse 3D morphologies (accordion-like, carambola-shaped, rosette pillar-shaped).
Conclusions:
- Resolved bond orthogonality issues in peptide-based supramolecular reconfiguration.
- Provided a versatile strategy for constructing morphologically controllable nanostructures.
- Paved the way for advanced peptide nanodevices through controlled reconfiguration.
Related Concept Videos
Protein Folding
129.5K
Overview
129.5K
Protein Folding
12.0K
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
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
12.0K

