Yeast two hybrid assay
Peptides are synthetically accessible, amenable to chemical tailoring, and have the potential to bind the typically shallow surfaces seen in therapeutically relevant—and historically intractable—protein–protein interactions (PPIs). Peptides can either act as natural ligands in the form of cofactors, coenzymes, and hormones, or directly interact with macromolecules including proteins, RNA, or DNA.
The antigen-binding capacity of nanobodies is similar to conventional antibodies for three reasons. First, the complementarity-determining region 3 (CDR3) of nanobodies is similar or even longer than that of human VH domain (variable domain of heavy immunoglobulin chain). Second, nanobodies can form finger-like structures to recognize cavities or hidden epitopes that are not available to mAbs.
The most common yeast display system employs fusion of the protein of interest to the C-terminus of the a-agglutinin mating protein Aga2p subunit, a technology pioneered by Boder and Wittrup. The yeast surface display construct designed for this system includes two epitope tags: a hemagglutinin (HA) tag between Aga2p and the N-terminus of the protein of interest, and a C-terminal c-myc tag.
Saccharomyces cerevisiae belongs to eukaryote, which is closer to the expression system of plants and animals. This expression system includes the following processes: glycosylation, disulfide bond formation, and Post-translational modification of protein folding.
The yeast two hybrid assay has emerged as a critical tool in the field of pharmaceuticals, particularly in the study of protein-protein interactions
The Yeast Two Hybrid Assay has emerged as a powerful tool in the discovery of new drug targets
In the yeast two hybrid assay, two proteins of interest are separately fused to different components of a transcription factor
Yeast Two Hybrid Assay has emerged as a powerful tool in functional genomics, enabling scientists to investigate protein-protein interactions with unparalleled precision
Yeast Two Hybrid Assay is a revolutionary technique widely employed in biopharmaceutical research to investigate protein-protein interactions