Abstract
“The power of evolution is revealed through the diversity of life,” says the announcement for the 2018 Nobel Prize in chemistry, George Smith described phage display technology in 1985, and it has since been expanded to include the display of peptides, various recombinant antibody formats, enzymes, and fragmented proteomes. These phage libraries can display a wide range of ligands on coat proteins projecting from the surface of the bacteriophage particle, with the ligand-coat protein fusion encoded using either a phagemid or phage vector system. Most phages have a high affinity for host cell surface receptors, such as receptor binding proteins (RBPs) or lipopolysaccharides (LPS). Recently, a number of real-time PCR assays for the rapid, sensitive, and specific detection of each F-RNA phage genogroup have been developed and RNA is reverse-transcribed into cDNA, used for PCR of the encoded antibodies’ VH and VL chains. The human antibody repertoire evolved to recognize any target with sufficient specificity and affinity that used RT-PCR to amplify the VH and VK and Vλ chains. Antibody phage display is a versatile in vitro selection technology for identifying high-affinity antibodies specific to a wide range of antigens. Low solubility affects the bioavailability, immunogenicity, and effectiveness of mAbs.