Ph on-off switching of antibody-hapten binding by site-specificchemical modification of tyrosine

Dan S. Tawfik, Rachel Chap, Zelig Eshhar, Bernard S. Green*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

34 Scopus citations

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∼ 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

Original languageEnglish
Pages (from-to)431-434
Number of pages4
JournalProtein Engineering, Design and Selection
Volume7
Issue number3
DOIs
StatePublished - Mar 1994

Keywords

  • Antibody engineering
  • Binding regulation
  • Nitrotyrosine
  • Surface
  • Tetranitromethane
  • Thermal stability

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