Phage Display Antibody is the first developed methodology for high throughput screening of human therapeutic antibodies. There are other methods developed with time for fully human therapeutic antibodies say single B-Cell screen and next-generation genome sequencing. Yet, the Phage Display Antibody remains a key methodology for human antibody discovery as it has a prominent in vitro process. There are various other technologies when paired with phage display prove important for therapeutic antibody discovery.
Initially, the display of folded proteins on phage through phage coat proteins fusion was to identify the protein target sequence that binds to antibodies. Ironically, now the most common use of Phage Display Antibody is to discover antibodies against the targeted proteins. The vast antibody repertoire displayed phage along with the genetic sequences within, and the robust screening showed the various target antigens and rapid recovery of antibody-specific sequences concerning recombinant expression.
The utility shown by semi-synthetic and fully synthetic libraries over the years has been beyond targeting self-antigens. These libraries are capable of generating high-affinity antibodies against target antigens of a wide variety. An example of a high-affinity antibody is raxibacumab for inhalational anthrax treatment.
There has been an increase in the development of higher affinity antibodies more than the approved therapeutic antibodies with extremely high diversity synthetic libraries. The human Phage Display Antibody contributes to the production of multiple drug candidates for clinical development phases.
High affinity tends to strong immune response and the antibodies being generated indicate their therapeutic potential based on the non-protein targets. The Phage Display Antibody can be used to produce anti-carbohydrate antibodies in the nanomolar range with reasonable affinity.
The Phage Library can construct high-affinity and specificity anti-carbohydrate antibodies that have been under clinical analysis. The isolation of lipoprotein antibodies has a role in recombinant development through phage display and has the potential to determine the pathological role and help reverse the effects of the diseases.
The development of human antibodies holding the same specificity of antibodies blocking in the complement fixation inhibiting endogenous antibodies effect in animal models by phage display. Phage display is highly appropriate to develop anti-idiotypic antibodies, showing therapeutic potential binding and blocking naturally occurring autoantibodies effects.
The most vital advantage of Phage Display Antibody is the in vitro antibody identification process allowing selection methodologies, unlike in vivo antibody selection. The phage display has the selection and screening controlled on immobilized antigens. The specific antigen for direct selection has desired regions on the target that can help generate antibodies of choice.
Also, the binding affinity and rates of antibody recovery can be optimized independently with the progression of the application in the selection. These can be further studied as recombinant expressions on different targets that can lead to the construction of alternate functionalities.
We at GeNext Genomics have been actively participating in creating multiple Phage Display Antibody Libraries, which adds value to research and development with biologics. We have a team of professionals working together to develop high-quality recombinant protein, STAT3 protein, and other biologics to serve the industry’s demands and support high-quality research.