Phage display technology is a powerful technique for antibody discovery. It is often used to identify high-affinity interactions between antibody fragments (e.g. VHHs) and target proteins for the production of monoclonal antibodies. Originally developed in the mid-1980s, phage display is a key technology for antibody engineering, drug discovery, protein-protein interactions, and vaccine development.1
By genetically engineering the bacteriophage's coat protein, the VHH (heavy-domain camelid antibody fragment) sequence can be linked to the phage DNA, enabling the displayed antibody fragment to be encoded by the viral genome. This facilitates the production of a diverse library of phage particles, each carrying a different antibody fragment on its surface.
These phage display libraries screen the phage particles to identify antibodies that bind to specific target antigens in a process called panning, which involves repeated rounds of binding, washing, elution, and amplification. Once identified, these antibodies can be further optimized for improved affinity, specificity, and therapeutic properties. Additionally, phage display has facilitated the discovery of small peptide-based drugs and the identification of potential drug targets.
At Biointron, we are dedicated to accelerating antibody discovery, optimization, and production. Our team of experts can provide customized solutions that meet your specific research needs. Contact us to learn more about our services and how we can help accelerate your research and drug development projects.
Hammers, C. M., & Stanley, J. R. (2014). Antibody Phage Display: Technique and Applications. The Journal of Investigative Dermatology, 134(2), e17. https://doi.org/10.1038/jid.2013.521
The therapeutic efficacy of antibodies is closely related to their ability to recognize and bind specific epitopes on target antigens. Epitopes, or antigenic determinants, are a group of amino acids or other chemical groups that are part of a molecule to which an antibody attaches itself. Epitope characterization can help reveal the mechanism of antibody binding and apply intellectual property (patent) protection for novel antibodies, in addition to designing antibodies with high specificity and minimal cross-reactivity.
Understanding the differences between antibody specificity and selectivity is essential for designing and interpreting antibody-based assays in research for experimental accuracy and data interpretation. Antibody specificity refers to an antibody's ability to recognize and bind to a particular epitope—a unique part of an antigen that elicits an immune response.
Antibody-based assays are essential tools in biomedical research, providing the means to detect, quantify, and visualize specific proteins or antigens within complex biological samples. These assays' efficacy hinges on the antibodies' precise properties. While affinity, avidity, specificity, and selectivity are fundamental to antibody performance, the ultimate impact of these properties is heavily influenced by the experimental context in which the antibody is employed.
Biologics, particularly antibodies, have become indispensable in biomedical research and therapeutic development. Research-use-only (RUO) biologics play a pivotal role in preclinical studies, providing researchers with the necessary tools to explore antibody functions and therapeutic potential in vivo.
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