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Screening and Identification of Small Peptides Targeting Fibroblast Growth Factor Receptor2 using a Phage Display Peptide Library

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Phage display peptide libraries: deviations from randomness and correctives.

Arie Ryvkin¹, Haim Ashkenazy¹, Yael Weiss-Ottolenghi¹

¹Department of Cell Research and Immunology, George S. Wise Faculty of Life Sciences, Tel Aviv University, Tel Aviv 69978, Israel.

Nucleic Acids Research

|February 9, 2018

Summary

This summary is machine-generated.

Phage display libraries are crucial for antibody research but often lack random amino acid representation. This study corrects biases in UAG codons and guanine abundance, ensuring reliable peptide selection for epitope discovery.

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Area of Science:

Molecular Biology
Biotechnology
Immunology

Background:

Peptide-expressing phage display libraries are essential tools for antibody interrogation and epitope mapping.
A key assumption for phage display applications is the random distribution of amino acids in naïve libraries.
Previous studies revealed significant deviations from randomness in naïve libraries, impacting downstream analyses.

Purpose of the Study:

To identify and rectify the causes of non-random amino acid distribution in phage display libraries.
To improve the reliability of phage display biopanning for epitope discovery and antibody interrogation.

Main Methods:

Utilized next-generation sequencing to analyze naïve peptide libraries for amino acid distribution biases.
Investigated the role of UAG codon over-representation and high guanine phosphoramidite abundance.
Employed supE44-containing bacteria to suppress UAG-driven termination and compensating oligonucleotide mixtures to correct guanine abundance.

Main Results:

Demonstrated that UAG over-representation is linked to phage assembly burdens, corrected by using supE44-containing bacteria.
Identified guanine overabundance as a result of variant synthesis-efficiency, corrected using mass spectrometry-calibrated oligonucleotide mixtures.
Constructed improved phage display libraries exhibiting random amino acid distribution.

Conclusions:

Correcting UAG codon and guanine biases significantly enhances the randomness of peptide libraries.
These improvements ensure that peptides selected during biopanning accurately reflect genuine selection events.
The optimized libraries provide a more reliable foundation for epitope discovery and antibody research using phage display technology.