pH on-off switching of antibody-hapten binding by site-specific chemical modification of tyrosine

Protein Eng. 1994 Mar;7(3):431-4. doi: 10.1093/protein/7.3.431.

Abstract

Tetranitromethane (TNM) chemically mutates the binding sites of antibodies so that the nitrated antibodies exhibit pH-dependent binding near physiological pH. Three monoclonal antibodies were selectively modified, each under different conditions, with the resultant loss of binding activity at pH > 8 which is recovered at pH < 6. Recovery and loss of binding are ascribed to the protonation and deprotonation, respectively, of the hydroxyl group of the resulting 3-nitrotyrosine side chain (pKa approximately 7) at the binding site of these antibodies. pH on-off dependency of binding activity, common to all TNM-modified antibodies studied by us so far, may find use in a variety of applications in which controlled modulation under mild conditions is required.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • 2,4-Dinitrophenol
  • Antibodies, Monoclonal / metabolism*
  • Binding Sites, Antibody / drug effects
  • Dinitrophenols / immunology
  • Haptens / metabolism*
  • Hemocyanins / metabolism
  • Hydrogen-Ion Concentration
  • Tetranitromethane / pharmacology*
  • Tyrosine / chemistry*

Substances

  • Antibodies, Monoclonal
  • Dinitrophenols
  • Haptens
  • Tyrosine
  • Hemocyanins
  • keyhole-limpet hemocyanin
  • Tetranitromethane
  • 2,4-Dinitrophenol