Detailed Explanation
Technique in which peptides are genetically fused to coat proteins of bacteriophages (viruses that infect bacteria), creating a physical link between the displayed peptide and the DNA that encodes it. A library of billions of phage particles, each displaying a different peptide, is screened against a target by 'biopanning': the library is exposed to the target, non-binders are washed away, and phages that stick are amplified by infecting bacteria.
After 3–5 rounds of selection, the enriched phages are sequenced to identify high-affinity peptide binders. Developed by George Smith in 1985 and applied to antibody engineering by Gregory Winter, phage display earned them the Nobel Prize in Chemistry in 2018. It is the most widely used method for discovering peptide ligands and therapeutic antibodies.
Key Facts
- Technique in which peptides are genetically fused to coat proteins of bacteriophages (viruses that infect bacteria), creating a physical link between the displayed peptide and the DNA that encodes it.
- A library of billions of phage particles, each displaying a different peptide, is screened against a target by 'biopanning': the library is exposed to the target, non-binders are washed away, and phages that stick are amplified by infecting bacteria.
- After 3–5 rounds of selection, the enriched phages are sequenced to identify high-affinity peptide binders.
- Developed by George Smith in 1985 and applied to antibody engineering by Gregory Winter, phage display earned them the Nobel Prize in Chemistry in 2018.
- It is the most widely used method for discovering peptide ligands and therapeutic antibodies.
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