Peptide ligands for a sugar-binding protein isolated from a random peptide library.
Peptide ligands for the carbohydrate-binding protein concanavalin A (Con A) have been identified by screening a large, diverse peptide library expressed on the surface of filamentous phage. A dodecapeptide containing the consensus sequence Tyr-Pro-Tyr was found to bind Con A with an affinity (dissociation constant, Kd) of 46 microM, comparable to that of a known carbohydrate ligand, methyl alpha-D-mannopyranoside (Kd of 89 microM). In addition the peptide inhibited precipitation of the alpha-glucan dextran 1355 by Con A. Given the complexity of oligosaccharide synthesis, the prospect of finding peptides that competitively inhibit carbohydrate-specific receptors may simplify the development of new therapeutic agents.
Oldenburg
K R
KR
Department of Bioorganic Chemistry, Affymax Research Institute, Palo Alto, CA 94304.
Loganathan
D
D
Goldstein
I J
IJ
Schultz
P G
PG
Gallop
M A
MA
D000595:Amino Acid Sequence; D001483:Base Sequence; D001665:Binding Sites; D002846:Chromatography, Affinity; D003090:Coliphages / Q000235:genetics; D003208:Concanavalin A / Q000737:chemistry / Q000378:metabolism*; D004247:DNA / Q000235:genetics; D003956:Dialysis; D008024:Ligands; D008969:Molecular Sequence Data; D009838:Oligodeoxyribonucleotides / Q000737:chemistry*; D009842:Oligopeptides / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D011485:Protein Binding; D013056:Spectrophotometry, Ultraviolet
D008024:Ligands; D009838:Oligodeoxyribonucleotides; D009842:Oligopeptides; D003208:Concanavalin A; D004247:DNA