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Synthesis of Information-bearing Peptoids and their Sequence-directed Dynamic Covalent Self-assembly
Published on: February 6, 2020
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Two-dimensional honeycomb network through sequence-controlled self-assembly of oligopeptides
Sabine Abb1, Ludger Harnau, Rico Gutzler1
1Max Planck Institute for Solid State Research, Heisenbergstraße 1, 70569 Stuttgart, Germany.
Nature Communications
|January 13, 2016
Summary
Peptide sequence controls self-assembly into 2D nanostructures. Sequence modification transforms compact assemblies into ordered chiral honeycomb networks, enabling bio-inspired surface design.
Area of Science:
- Biomaterials Science
- Nanotechnology
- Surface Chemistry
Background:
- Peptide sequence dictates self-assembly via non-covalent interactions.
- Various peptide nanostructures have been designed using interactions like hydrogen bonding and ionic forces.
Purpose of the Study:
- To demonstrate sequence-controlled fabrication of 2D molecular nanostructures using peptides.
- To investigate how sequence modification affects peptide self-assembly.
- To elucidate interpeptide-binding motifs for rational design.
Main Methods:
- Utilizing peptides as bio-organic building blocks for 2D self-assembly.
- Employing Scanning Tunneling Microscopy (STM) to observe nanostructure formation.
- Conducting molecular dynamic simulations to model atomistic details.
Main Results:
- Sequence modification of peptides led to distinct self-assembly patterns.
- Angiotensin I formed compact or linear assemblies, while angiotensin II formed ordered, chiral honeycomb networks.
- STM revealed a transition from disordered to long-range ordered structures upon sequence alteration.
Conclusions:
- Peptide sequence modification is a powerful tool for controlling 2D self-assembly.
- This approach allows for the creation of complex, bio-inspired nanostructures.
- The findings enable the rational design of surfaces using polypeptides as functional building blocks.
