ABSTRACT

Phage-displayed peptide libraries can be used to isolate specific, high-affinity peptides to almost any protein target. Peptides have been identified for a wide range of protein targets including antibodies (1,2), enzymes (3,4), G proteins (5), nuclear receptors (6,7), cytokine receptors (8,9), cytokines (10), transcription factors (11), and protein interaction domains (12-14). The peptides identified by affinity selection from phage-displayed peptide libraries bind to biologically relevant sites on these target proteins and therefore can serve as

valuable reagents for dissecting the biological function of proteins as well as tools for drug discovery.