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.
Wong
D W
DW
Western Regional Research Center, USDA-ARS, 800 Buchanan Street, Albany, California 94710, USA.
Robertson
G H
GH
Tillin
S J
SJ
Wong
C
C
D000595:Amino Acid Sequence; D000818:Animals; D016384:Consensus Sequence; D001467:Hordeum / Q000201:enzymology*; D008024:Ligands; D008969:Molecular Sequence Data; D010179:Pancreas / Q000201:enzymology*; D019151:Peptide Library; D010455:Peptides / Q000737:chemistry* / Q000378:metabolism*; D011485:Protein Binding; D013552:Swine; D000516:alpha-Amylases / Q000378:metabolism*
D008024:Ligands; D019151:Peptide Library; D010455:Peptides; D000516:alpha-Amylases