Efficient isolation of peptide ligands for the endothelial cell protein C receptor (EPCR) using candidate receptor phage display biopanning.
Phage display biopanning has been used for a number of applications including ligand generation for targeted drug delivery, targeting gene therapy vectors and identification of protein-protein interaction sites. In this study, a random phage display library was used to isolate peptide ligands to the endothelial protein C receptor (EPCR), identifying 74 different peptide sequences and several motifs. Binding to EPCR was characterized by a solid phase binding assay, demonstrating that 95% of isolated peptides were specific for EPCR. Several homologies with potential relevance to EPCR biology were identified, the most notable being leukolysin (MT-MMP6) and cerastocytin.
White
Stephen J
SJ
Bristol Heart Institute, University of Bristol, Level 7 Bristol Royal Infirmary, Bristol BS2 8HW, UK. steve.white@bris.ac.uk
Simmonds
Rachel E
RE
Lane
David A
DA
Baker
Andrew H
AH
D000595:Amino Acid Sequence; D001665:Binding Sites; D001779:Blood Coagulation Factors / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D002478:Cells, Cultured; D015870:Gene Expression; D006801:Humans; D008024:Ligands; D008969:Molecular Sequence Data; D019151:Peptide Library; D010455:Peptides / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification*; D011956:Receptors, Cell Surface / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D014162:Transfection
D001779:Blood Coagulation Factors; D008024:Ligands; D019151:Peptide Library; D010455:Peptides; D011956:Receptors, Cell Surface; C091963:activated protein C receptor