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Related Experiment Video

Updated: Jul 18, 2025

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

Enzyme-Driven, Switchable Catalysis Based on Dynamic Self-Assembly of Peptides.

Qing Li¹, Jiwei Min¹, Jiaxing Zhang¹

¹State Key Laboratory of Chemical Engineering, School of Chemical Engineering and Technology, Tianjin University, Tianjin, 300072, P. R. China.

Angewandte Chemie (International Ed. in English)

|August 21, 2023

Summary

Researchers developed switchable peptide-based catecholase mimetics using copper ions (Cu²⁺) and self-assembling nanofibers. This biomimetic enzyme design offers dynamic control over catalytic activity and ordered structures.

Keywords:

Dynamic Self-Assembly Enzyme Mimics Enzyme-Driven Phosphorylation Switch Switchable Catalysis

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Area of Science:

Biomimetic chemistry
Supramolecular chemistry
Enzyme catalysis

Background:

Enzyme activity is modulated by covalent regulatory systems.
Inspired by biological phosphorylation, peptide-based systems offer tunable catalytic functions.

Purpose of the Study:

To develop peptide-based catecholase mimetics with switchable catalytic activity.
To engineer self-assembling nanofibers for controlled enzyme mimicry.

Main Methods:

Co-assembly of peptide and copper ions (Cu²⁺) into nanofibers.
Utilizing kinase/phosphatase switches for reversible control of nanofiber formation.
Coarse-grained molecular dynamics simulations and theoretical calculations.

Main Results:

Identified peptide structures with effective reversible catalytic activity.
Confirmed zipper-like four-ligand structure of peptide-Cu²⁺ at the active site.
Demonstrated dynamic modulation of catalytic activity through nanofiber assembly/disassembly.

Conclusions:

Novel peptide-based catecholase mimetics with switchable activity were successfully designed.
The study provides a framework for creating biomimetic enzymes with dynamic and ordered structures.
Opens new avenues for designing responsive catalytic systems.