Phage display technology is a technique based on the display of exogenous peptides, antibodies or proteins on the surface of phages. The technique was first reported by George P. Smith et al. in 1985 and was applied in the field of antibody engineering by John McCafferty and Gregory Winter in the early 1990s. Since then, it has been continuously improved and refined, and has become one of the important tools in the field of modern biomedical research. In 2018, two pioneers in phage display research, American scientist George P. Smith and British scientist Gregory P. Winter, were awarded the Nobel Prize in Chemistry.

In phage display technology, exogenous proteins or peptide sequences are cloned into specific regions of phage surface proteins, thereby displaying them on the phage surface. Subsequently, phages in the phage library can be used to screen out antibodies or proteins that bind to target molecules. This technology can screen antibodies or proteins with specificity in high throughput, and thus is widely used in new drug discovery, antibody screening, vaccine development and other fields.

Mechanism of Phage Display

Phage display technology is the insertion of exogenous peptides, antibodies, and other fragments, into the structural genes of the phage, commonly expressed in fusion with PIII or PVIII, and the molecules displayed on the surface of the phage remain biologically active. To select the desired molecules from the phage library, it is necessary to go through ‘panning’. The process simply means that the peptide or protein libraries presented on the phage surface are able to specifically recognize and bind to the target antigen, and after sufficient incubation time, free phages with weak or unbound antigen binding can be washed away using a washing solution. The specifically bound target phages are then eluted, infected with E. coli and amplified to obtain the next round of sub-phage libraries. Subsequently, after two to three rounds of ‘adsorption-elution-amplification’ enrichment, the proportion of phage that can specifically bind to the antigen was gradually increased. Peptides or proteins that can recognize the target molecule are finally obtained and can be used in subsequent experiments. 

Advantages of Phage Display Technology

High throughput: phage display technology can display thousands of different antibodies or proteins at the same time, which can greatly speed up screening and improve efficiency.

Stability: Phage antibody libraries can be stored and used for long periods of time, thus enabling long-term research and development efforts.

Flexibility: Phage display technology can be used to display various types of molecules, including antibodies, proteins, peptides, etc., and thus has a wide range of application prospects.

Low cost: Phage display technology is performed based on a prokaryotic platform and eliminates the need for complex instrumentation and expensive reagents, making it the first choice for nanobody development. 

Phage Display Platform of Kanghui-Bio

• Own alpaca base
• Years of R&D experience
• Optimized display system
• Multiple selection methods
• Short cycle time, high storage capacity