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Phage Display Technology

Definition:

Phage display technology is a powerful bioengineering method used to study protein-protein interactions and to screen for high-affinity proteins or peptides. This technique was originally developed by George P. Smith in 1985, utilizing phages—a type of virus that infects bacteria—to display random peptide sequences or protein libraries. Below are the basic principles and steps of phage display technology: Gene Engineering: First, the gene sequence of the target protein or peptide is inserted into the phage genome, usually into the gene for the phage coat protein (such as pIII or pVIII). This allows the target protein or peptide to be displayed as part of the phage coat protein on the surface of the phage.
Phage Replication and Expression: The modified phages infect host bacteria (typically E. coli), replicate, and express the new coat protein, displaying the target protein or peptide on the surface.
Screening and Selection: These display phages are exposed to the target ligand (which can be a protein, DNA, small molecule, etc.) for binding. Unbound phages are washed away, leaving only those that have bound to the target ligand.
Elution and Amplification: The phages bound to the ligand are eluted using specific methods, then the host bacteria are re-infected for amplification, preparing for the next round of selection.
Iterative Screening: The screening process is repeated for multiple rounds (typically 3-5 rounds) to enrich the phage library for proteins or peptides with high-affinity interactions with the target ligand.
Sequencing: Finally, the selected phages are sequenced to identify the exact sequence of the protein or peptide that successfully bound to the target ligand.

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