Phage-displayed peptide ligands for pancreatic alpha-amylase cross-react with barley alpha-amylase

Peptide ligands that bind to pancreatic a-amylase were isolated from bacter iophage libraries displaying random 15-mer peptides by iterative affinity s election and amplification. The DNA sequences of selected clones from the f inal round of biopanning were determined. The two phage-display ligands wit h high-binding activities contained a high content of Arg, Tyr, and Trp res idues with the short consensus sequence Arg-X-Tyr-Trp. These clones were sh own to exhibit comparable binding interactions toward barley a-amylase base d on transducing units titering and measurement of the dissociation constan ts.