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Related Experiment Video

Updated: May 2, 2026

Using Phage Display to Develop Ubiquitin Variant Modulators for E3 Ligases

Using Phage Display to Develop Ubiquitin Variant Modulators for E3 Ligases

Published on: August 27, 2021

Dual genetically encoded phage-displayed ligands.

Kritika Mohan¹, Gregory A Weiss²

¹Department of Chemistry, University of California, Irvine, Irvine, CA 92697, USA.

Analytical Biochemistry

|March 11, 2014

Summary

This study introduces a modified phage propagation protocol for enhanced display of ligands on M13 bacteriophages. The research shows that phage surfaces have a saturation point for optimal peptide display, crucial for biosensor development.

Keywords:

Bacterial transformation ELISA Phage Phage display

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Last Updated: May 2, 2026

Using Phage Display to Develop Ubiquitin Variant Modulators for E3 Ligases

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Area of Science:

Molecular biology
Biotechnology
Biophysics

Background:

M13 bacteriophage display technology utilizes phage coat proteins to present polypeptides.
Phage-displayed ligands are valuable reagents for developing advanced biosensors.

Purpose of the Study:

To develop a modified phage propagation protocol for consistent and robust display of multiple ligands.
To investigate the display capacity of the M13 bacteriophage surface.

Main Methods:

Genetic encoding of two distinct ligands as fusions to the major coat protein (P8) of M13 bacteriophage.
Optimization of phage propagation to achieve high-density ligand display.

Main Results:

Demonstrated consistent and robust display of genetically encoded ligands on the P8 coat protein.
Identified a saturation point for maximum peptide display on the phage surface.

Conclusions:

The modified protocol enables efficient and reproducible display of multiple ligands on M13 bacteriophages.
Understanding phage surface saturation is key for maximizing ligand presentation in biosensor applications.