PHAGE DISPLAY OF PROTEINS

In recent years the phage display approach has become an increasingly popular method in protein research. This method enables the presentati on of large peptide and protein libraries on the surface of phage part icles from which molecules of desired functional property(ies) can be rapidly selected. The great advantage of this method is a direct linka ge between an observed phenotype and encapsulated genotype, which allo ws fast determination of selected sequences. The phage display approac h is a powerful tool in generating highly potent biomolecules, includi ng: search for specific antibodies, determining enzyme specificity, ex ploring protein-protein and protein-DNA interactions, minimizing prote ins, introducing new functions into different protein scaffolds, and s earching sequence space of protein folding. In this article many examp les are given to illustrate that this technique can be used in differe nt fields of protein science. The phage display has a potential of the natural evolution and its possibilities are far beyond rational predi ction. Assuming that we can design the selection agents and conditions we should be able to engineer any desired protein function or feature .