Introduction
Phage display is a versatile molecular biology technique that enables the presentation of peptides, antibodies, or proteins on the surface of bacteriophages (viruses that infect bacteria). This technology, first developed by George P. Smith in 1985, has revolutionized protein engineering, epitope mapping, and drug discovery by allowing researchers to screen vast libraries of biomolecules for specific binding interactions.
How Phage Display Works
The process involves genetically fusing a gene encoding a target protein or peptide to a phage coat protein gene. When the phage replicates, the foreign protein is displayed on its surface while its DNA remains encapsulated inside. This linkage between phenotype (displayed protein) and genotype (encoded DNA) allows for rapid selection and amplification of desired variants through biopanning—a process where phages are exposed to a target (e.g., an antigen, receptor, or small molecule), unbound phages are washed away, and bound phages are eluted and amplified in bacteria for subsequent rounds of selection.
Applications of Phage Display
Antibody Discovery – Phage display is widely used to generate monoclonal antibodies for therapeutic and diagnostic purposes.
Peptide Engineering – Researchers identify high-affinity peptides for drug delivery, diagnostics, and biomaterials.
Protein-Protein Interactions – The technique helps map binding sites and optimize protein interactions.
Vaccine Development – Phage display aids in identifying immunogenic epitopes for vaccine design.
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Conclusion
Phage display continues to be a cornerstone technology in biotechnology, enabling rapid discovery and optimization of biomolecules. Its applications span therapeutics, diagnostics, and basic research, making it indispensable in modern science.
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