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Related Experiment Video

Updated: Sep 12, 2025

Profiling Ubiquitin and Ubiquitin-like Dependent Post-translational Modifications and Identification of Significant Alterations

Profiling Ubiquitin and Ubiquitin-like Dependent Post-translational Modifications and Identification of Significant Alterations

Published on: November 7, 2019

Characterizing and engineering post-translational modifications with high-throughput cell-free expression.

Derek A Wong^1,2,3, Zachary M Shaver^2,3,4,5, Maria D Cabezas^1,2,3

¹Department of Chemical and Biological Engineering, Northwestern University, Evanston, IL, 60208, USA.

Nature Communications

|August 5, 2025

Summary

This summary is machine-generated.

A new workflow rapidly tests proteins that install post-translational modifications (PTMs). This method accelerates the engineering of therapeutic peptides and glycoproteins by improving design-build-test-learn cycles.

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Last Updated: Sep 12, 2025

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Published on: November 7, 2019

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High Yield Expression of Recombinant Human Proteins with the Transient Transfection of HEK293 Cells in Suspension

High Yield Expression of Recombinant Human Proteins with the Transient Transfection of HEK293 Cells in Suspension

Published on: December 28, 2015

Area of Science:

Biochemistry
Molecular Biology
Protein Engineering

Background:

Post-translational modifications (PTMs) are crucial for the stability and function of therapeutic proteins and peptides.
Existing methods for studying and engineering PTMs are often low-throughput and experimentally intensive.

Purpose of the Study:

To develop a generalizable, in vitro workflow for rapid expression and testing of PTM-installing proteins.
To apply this workflow to ribosomally synthesized and post-translationally modified peptides (RiPPs) and glycoproteins.
To accelerate the engineering of PTMs for therapeutic applications.

Main Methods:

Coupling cell-free gene expression (CFE) with AlphaLISA for high-throughput protein analysis.
Characterizing RiPP recognition elements and integrating into biodiscovery pipelines.
Adapting the workflow to study and engineer oligosaccharyltransferases (OSTs) for glycoprotein production.

Main Results:

Demonstrated workflow for characterizing RiPP recognition element binding activity.
Successfully integrated workflow into a biodiscovery pipeline for RiPP products.
Identified mutant OSTs and specific sites on a model vaccine carrier protein for efficient glycosylation.
Enabled high-efficiency production of glycosylated proteins.

Conclusions:

The developed CFE-AlphaLISA workflow provides a rapid and generalizable method for studying and engineering PTMs.
This approach significantly accelerates the design-build-test-learn cycles in protein and peptide therapeutic engineering.
The workflow has broad applicability, particularly for RiPPs and glycoproteins, advancing therapeutic development.