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Related Experiment Videos

Sequence-specific peptide cleavage catalyzed by an antibody.

B L Iverson1, R A Lerner

  • 1Department of Molecular Biology, Research Institute of Scripps Clinic, La Jolla, CA 92037.

Science (New York, N.Y.)
|March 3, 1989
PubMed
Summary

Antibodies were engineered to catalyze peptide bond hydrolysis using metal cofactors. This demonstrates cofactor-assisted catalysis within antibody binding sites for complex chemical reactions.

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Area of Science:

  • Biochemistry
  • Immunology
  • Catalysis

Background:

  • Monoclonal antibodies typically bind antigens but can be engineered for catalytic activity.
  • Metal complexes can serve as cofactors to enhance antibody catalytic function.
  • Hydrolysis of specific peptide bonds presents a challenging chemical transformation.

Purpose of the Study:

  • To develop monoclonal antibodies capable of catalyzing specific peptide bond hydrolysis.
  • To investigate the role of metal complex cofactors in antibody-catalyzed reactions.
  • To demonstrate the feasibility of cofactor-assisted catalysis in antibody binding sites.

Main Methods:

  • Antibodies were generated by immunizing with a cobalt(III) triethylenetetramine-peptide hapten.
  • Various peptide substrates and metal complexes were screened for antibody-mediated cleavage.
  • Detailed kinetic analysis was performed on a specific antibody-substrate-cofactor system.

Main Results:

  • Monoclonal antibodies were successfully induced to catalyze Gly-Phe bond hydrolysis in peptide substrates.
  • Cleavage occurred at neutral pH with various metal complex cofactors (e.g., Zn(II), Cu(II), Fe(III)).
  • A turnover number of 6 x 10(-4) s⁻¹ was observed, indicating catalytic efficiency.

Conclusions:

  • Cofactor-assisted catalysis within antibody binding sites is feasible.
  • Engineered antibodies can perform challenging chemical transformations like peptide hydrolysis.
  • This approach offers a novel strategy for designing artificial enzymes.

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