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 language | English |
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Pages (from-to) | 431-434 |
Number of pages | 4 |
Journal | Protein Engineering, Design and Selection |
Volume | 7 |
Issue number | 3 |
DOIs | |
State | Published - Mar 1994 |
Keywords
- Antibody engineering
- Binding regulation
- Nitrotyrosine
- Surface
- Tetranitromethane
- Thermal stability