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Related Experiment Video

Updated: Jul 5, 2025

Creating Highly Specific Chemically Induced Protein Dimerization Systems by Stepwise Phage Selection of a Combinatorial Single-Domain Antibody Library

Creating Highly Specific Chemically Induced Protein Dimerization Systems by Stepwise Phage Selection of a Combinatorial Single-Domain Antibody Library

Published on: January 14, 2020

Omniligase-1-Mediated Phage-Peptide Library Modification and Insulin Engineering.

Yi Wolf Zhang^1,2, Nai-Pin Lin¹, Xu Guo³

¹Department of Pediatrics, Division of Diabetes and Endocrinology, Stanford University, Palo Alto, California 94304, United States.

ACS Chemical Biology

|January 24, 2024

Summary

This summary is machine-generated.

We developed a new phage display method using omniligase-1 for protein engineering. This technique successfully created insulin analogues with biological activity, paving the way for new therapeutics.

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Area of Science:

Biochemistry
Molecular Biology
Protein Engineering

Background:

Phage display is a powerful tool for protein engineering.
Current methods have limitations in epitope and scaffold specificity.
Expanding phage display capabilities is crucial for discovering novel therapeutics.

Purpose of the Study:

To introduce a novel omniligase-1-mediated ligation technique for phage display.
To engineer insulin analogues with modified B chain C-terminal regions.
To assess the biological activity and receptor interactions of engineered insulin analogues.

Main Methods:

Utilized omniligase-1 for selective and specific ligation on phage pIII protein.
Applied the method to high-throughput engineering of insulin analogues.
Performed molecular dynamics studies to analyze insulin analogue interactions.

Main Results:

Achieved high conversion rates and compatibility with commercial phage libraries.
Selected insulin analogues with biological activity equivalent to human insulin.
Discovered a novel interaction between insulin B27 and the insulin receptor L1 domain.

Conclusions:

Omniligase-1-mediated phage display is effective for engineering disulfide-rich proteins.
This approach enables the development of novel insulin analogues with therapeutic potential.
The method shows promise for creating other therapeutic compounds.