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Updated: May 5, 2026

A New Screening Method for the Directed Evolution of Thermostable Bacteriolytic Enzymes

A New Screening Method for the Directed Evolution of Thermostable Bacteriolytic Enzymes

Published on: November 7, 2012

Directed Evolution Using Stabilized Bacterial Peptide Display.

Tejas Navaratna¹, Lydia Atangcho¹, Mukesh Mahajan¹

¹Department of Chemical Engineering , University of Michigan , Ann Arbor , Michigan 48109 , United States.

Journal of the American Chemical Society

|December 28, 2019

Summary

This summary is machine-generated.

Chemically stabilized peptides offer new ways to target difficult diseases. A new method rapidly isolates high-affinity peptides with improved drug-like properties, accelerating drug discovery for challenging targets.

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Area of Science:

Biochemistry
Molecular Biology
Drug Discovery

Background:

Chemically stabilized peptides are promising for targeting

Purpose of the Study:

To develop a method for rapid isolation of stabilized peptides with high affinity and drug-like properties.
To apply this method to discover inhibitors of the MDM2-p53 interaction.

Main Methods:

Incorporation of non-natural amino acids and cell surface click chemistry in bacteria.
High-throughput sorting and quantitative selection of high-affinity ligands.
Application of the Stabilized Peptide Evolution by *E. coli* Display technique.

Main Results:

Rapid isolation of stabilized peptides with improved affinity and novel structures.
Identification of a bicyclic peptide with a K_d of 1.8 nM and enhanced protease stability.
Demonstration of protease resistance measurement on bacterial surfaces and in solution.

Conclusions:

The developed method enables rapid isolation of stabilized peptides with enhanced affinity and drug-like properties.
This technique accelerates the discovery of therapeutics for previously undruggable targets.
The method can be used to screen for additional drug-like properties critical for therapeutic development.