ABSTRACT
Phage display technology provides a remarkably versatile tool for exploring the interactions between proteins, peptides, and small-molecule ligands. As such, it has become widely adapted for use in epitope mapping, identication of protein-peptide and protein-protein interactions, protein-small molecule interactions, humanization of antibodies, identication of tissue-targeting peptides, and many other applications as outlined throughout this book. However, it must be kept in mind that phage display is a combinatorial biology approach, not a combinatorial chemistry approach. The great strength of phage display over combinatorial methods that are strictly chemical is that the isolation of a single interacting protein or peptide attached to a phage particle is sufcient to allow the complete characterization of the isolate: the interacting virus can be grown up in bulk and the sequence of the displayed protein or peptide inferred from the DNA sequence carried within the viral particle. The other side of this coin is that phage display technology utilizes living systems, and is therefore constrained in its potential diversity by the molecular requirements of those systems.
