Identification and characterization of a TNF alpha antagonist derived from a monoclonal antibody

Mol Immunol. 1994 Oct;31(14):1059-67. doi: 10.1016/0161-5890(94)90101-5.

Abstract

Peptides derived from the CDRs of the anti-TNF alpha monoclonal antibody Di62 were tested for inhibition of binding of Di62 to TNF alpha as well as of TNF alpha to its 55 and 75 kDa receptor. A peptide derived from the CDR1 of the light chain was shown to specifically inhibit Di62 binding to TNF alpha with markedly higher activity (Ki = 4 microM) than all other CDR-derived peptides. This peptide also significantly inhibited binding of TNF alpha to its 55 and 75 kDa receptor and protected L929 cells from the cytotoxic effect of TNF alpha (IC50 = 6 microM). The C-terminal region of this peptide, which is homologous to the 55 and 75 kDa TNF receptor, was found to be essential for activity.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Antibodies, Monoclonal / immunology*
  • Binding, Competitive / immunology
  • Cytotoxicity Tests, Immunologic
  • Enzyme-Linked Immunosorbent Assay
  • Immunoglobulin Variable Region / immunology*
  • L Cells
  • Mice
  • Molecular Sequence Data
  • Mutagenesis, Site-Directed
  • Radioimmunoassay
  • Receptors, Tumor Necrosis Factor / immunology
  • Tumor Necrosis Factor-alpha / antagonists & inhibitors
  • Tumor Necrosis Factor-alpha / immunology*

Substances

  • Antibodies, Monoclonal
  • Immunoglobulin Variable Region
  • Receptors, Tumor Necrosis Factor
  • Tumor Necrosis Factor-alpha