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A Protocol for Phage Display and Affinity Selection Using Recombinant Protein Baits
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A novel phage display vector for selection of target-specific peptides
Alex Chang1, Joey P Ting2, Alfonso Espada3
1Department of Pharmacy, Santa Clara Valley Medical Center, San Jose CA 95128, USA.
Protein Engineering, Design & Selection : PEDS
|October 3, 2020
Summary
Phage display limitations were overcome by increasing peptide display levels 30-fold. This was achieved by optimizing the PIII protein in a novel phage vector, aiding therapeutic peptide discovery.
Area of Science:
- Biotechnology
- Molecular Biology
- Protein Engineering
Background:
- Phage display technology is crucial for identifying specific binders.
- Low polypeptide display levels on phage limit binder isolation efficiency.
- Optimizing protein expression is key to enhancing phage display capabilities.
Purpose of the Study:
- To overcome the limitation of low polypeptide display levels in phage display.
- To engineer a novel phage vector for increased peptide presentation.
- To improve the efficiency of discovering therapeutic peptides.
Main Methods:
- Modification of the type 33 phage vector.
- Randomization of the first 67 amino acids of the wild-type PIII protein.
- Selection of mutants with reduced PIII expression for higher fusion protein incorporation.
Main Results:
- Achieved a 30-fold improvement in peptide display level on the phage surface.
- Demonstrated higher incorporation of a synthetic PIII-peptide fusion protein.
- Successfully engineered a phage vector with enhanced display capacity.
Conclusions:
- The novel phage vector significantly enhances peptide display levels.
- This advancement provides a robust platform for therapeutic peptide discovery.
- Optimized PIII expression is critical for improving phage display applications.
