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Phage peptide display technology was not initially designed to develop cyclic peptide compounds when it was first introduced [1]. In this technology, each phage particle displays a unique peptide on its surface and the winner can be selected for binding toward a target molecule. Usually, peptides are displayed on the N-terminus, the middle, or the C-terminus of coat proteins, and the peptide sequence from each phage particle is directed by the DNA sequence of the same phage particle, allowing an easy sequence determination. The selection can be repeated as long as encoding DNA molecules are preserved, and this repeated procedure, called biopanning, is used to enrich the best binders. Billions of pooled peptides presented on phage particles form a phage displayed peptide library, and in contrast to regular synthetic small molecule libraries, as many as 10 different peptides can be screened simultaneously for the desired activity [2].

From Bench to Clinical Using a Combinatorial Screenings of Phage-Displayed Peptide Libraries