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Related Experiment Video

Updated: Oct 7, 2025

OaAEP1-Mediated Enzymatic Synthesis and Immobilization of Polymerized Protein for Single-Molecule Force Spectroscopy

OaAEP1-Mediated Enzymatic Synthesis and Immobilization of Polymerized Protein for Single-Molecule Force Spectroscopy

Published on: February 5, 2020

Enzymatic C-to-C Protein Ligation.

Fabian B H Rehm¹, Tristan J Tyler¹, Simon J de Veer¹

¹Institute for Molecular Bioscience, Australian Research Council Centre of Excellence for Innovations in Peptide and Protein Science, The University of Queensland, Brisbane, QLD 4072, Australia.

Angewandte Chemie (International Ed. in English)

|January 12, 2022

Summary

This summary is machine-generated.

Researchers engineered an asparaginyl ligase for novel C-to-C protein and peptide ligations. This breakthrough overcomes the traditional N-to-C limitation, expanding possibilities in bioconjugation and therapeutic development.

Keywords:

Biorthogonal Enzyme Bioconjugation Enzyme Catalysis Protein Engineering Site-Specificity

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Synthesis of Protein Bioconjugates via Cysteine-maleimide Chemistry

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Synthesis of Protein Bioconjugates via Cysteine-maleimide Chemistry

Synthesis of Protein Bioconjugates via Cysteine-maleimide Chemistry

Published on: July 20, 2016

Area of Science:

Biochemistry
Synthetic Biology
Protein Engineering

Background:

Transpeptidase enzymes are crucial for protein and peptide modification, enabling the creation of conjugates for research and therapeutics.
Current transpeptidases are limited to N-to-C ligation, restricting the diversity of achievable products.

Purpose of the Study:

To overcome the N-to-C ligation constraint of transpeptidases.
To develop a novel enzyme-catalyzed method for C-to-C protein and peptide ligation.

Main Methods:

Engineered an asparaginyl ligase to accept diverse nucleophile substrate mimetics.
Developed a strategy to quench byproduct reactivity.
Utilized C-terminal Leu-ethylenediamine (Leu-Eda) as a mimic for native N-terminal sequences.
Applied the method to synthetic peptides and recombinant proteins via intein splicing.

Main Results:

The engineered ligase successfully catalyzed C-to-C ligations.
Demonstrated the utility of Leu-Eda motifs as effective mimics.
Achieved direct transpeptidase-catalyzed C-to-C ligation of peptides and proteins.

Conclusions:

This work introduces a novel C-to-C ligation strategy using engineered asparaginyl ligases.
Significantly expands the synthetic capabilities of enzyme-catalyzed protein transpeptidation.
Opens new avenues for creating diverse bioconjugates and therapeutic agents.