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Updated: Mar 31, 2026

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

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

Published on: February 6, 2020

Reprogramming Chirality in Peptide Self-Assembly via Intramolecular Side Chain-Backbone Hydrogen Bonding.

Kai Qi^1,2, Yan Wang¹, Yu Han¹

¹Department of Biological and Energy Chemical Engineering, China University of Petroleum (East China), 66 Changjiang West Road, Qingdao 266580, China.

|March 30, 2026

Summary

This summary is machine-generated.

Uncharged polar amino acid side chains, like serine and threonine, can control peptide structure through hydrogen bonding. This interaction reprograms self-assembly, enabling the design of peptide materials with specific chirality.

Keywords:

chirality hydrogen bonding nanofiber peptide polar side chain self-assembly

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Area of Science:

Biochemistry
Supramolecular Chemistry
Materials Science

Background:

Protein structure is maintained by main chain-main chain and side chain-side chain interactions.
The role of main chain-side chain interactions, particularly with uncharged polar side chains, is underexplored.
Uncharged polar side chains can modulate conformation via hydrogen bonding (H-bonding) with the protein backbone.

Purpose of the Study:

To investigate the role of main chain-side chain H-bonding in peptide conformation and self-assembly.
To explore how uncharged polar side chains influence peptide conformational preferences.
To demonstrate a strategy for engineering peptide nanofibrils with specific chirality.

Main Methods:

Synthesis and analysis of 15 minimalistic amphiphilic peptides.
Investigation of intrastrand H-bonding between C-terminal side chains and the main chain.
Characterization of conformational preferences and β-sheet assembly modes.

Main Results:

Intrastrand H-bonding involving C-terminal uncharged polar side chains dictates peptide conformational preferences.
Serine and threonine side chains significantly alter single-strand conformations.
This alteration reprograms interstrand H-bonding in β-sheet assembly, leading to distinct right-handed supramolecular chirality.

Conclusions:

Polar side chain-backbone H-bonding is a key determinant of peptide chirality.
This mechanism provides a rational design strategy for creating peptide nanofibrils with controlled, rare right-handed chirality.
The findings advance the understanding of peptide self-assembly and biomaterial design.