Mapping an antibody binding site by nuclear decay

R. Mogul, C. F. Meares

Research output: Contribution to journalArticlepeer-review


The study of proteins and their complexes by cleavage of polypeptide chains provides a new approach to understanding their behavior in solution. Using radionuclides as the potential .source for this bond-breaking energy, we have assessed the effects of nuclear decay on two antibody binding sites. Monoclonal antibody CHA255 specifically binds para substituted (S)-benzyl-EDTA[In] chelates. Allowing CHA255 to bind a chelate containing the radioisotope In-111, which decays by electron capture, results in chain cleavage at several points within the binding pocket of the antibody. Correlation with the anti body/hapten crystal structure supports cleavage at or near the residues that either hydrogen bond to the hapten or directly coordinate the metal. In exper iments with a different monoclonal antibody that binds an yttrium chelate. we have found similar results from the energetic 2.2 MeV beta decay of yttriuin-90. Accurate assignment of these cleavage sites will provide calibration of the short range over which different modes of nuclear decay act to cleave polypeptides backbones.

Original languageEnglish (US)
JournalFASEB Journal
Issue number9
StatePublished - 1997

ASJC Scopus subject areas

  • Agricultural and Biological Sciences (miscellaneous)
  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry
  • Cell Biology


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