PMID: 2485226Nov 1, 1988Paper

Generation and characterization of specific antibodies directed to the binding domain of adhesive molecules

Peptide Research
S BerlinerZ M Ruggeri

Abstract

Antibodies were selected in rabbits using as immunogens five synthetic peptides representing the putative cell-binding domains of von Willebrand factor (vWF), fibrinogen (Fn), fibronectin (Fn) and vitronectin. All peptide immunogens contained the sequence Arg-Gly-Asp, thought to be involved in ligand binding to platelet glycoprotein (GP) IIb-IIIa; two of them corresponded to two distinct regions in the alpha-chain of fibrinogen. All anti-peptide antibodies recognized the corresponding immunogen, and four of them, i.e. all except the anti-vitronectin antibody, reacted with the native macromolecule containing the cognate sequence. Each antibody was specific for the corresponding adhesive protein and did not cross-react with any of the others in spite of the presence of the common sequence Arg-Gly-Asp. Two murine monoclonal antibodies reacting with the vWF peptide and with native vWF were used to define the amino acid residues involved in the antigen-antibody interaction. These residues included the glycine and aspartic acid residues of the common Arg-Gly-Asp sequence, as well as other residues specific to the vWF sequence. The antibodies were potent inhibitors of vWF binding to GP IIb-IIIa. The present studies demonstrate that th...Continue Reading

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