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

Peptide ligands that bind to pancreatic alpha-amylase were isolated from bacteriophage libraries displaying random 15-mer peptides by iterative affinity selection and amplification. The DNA sequences of selected clones from the final round of biopanning were determined. The two phage-display ligands with high-binding activities contained a high content of Arg, Tyr, and Trp residues with the short consensus sequence Arg-X-Tyr-Trp. These clones were shown to exhibit comparable binding interactions toward barley alpha-amylase based on transducing units titering and measurement of the dissociation constants.