History



           The concept that antibodies may catalyze chemical reactions was first proposed by Linus Pauling in the 40's. He suggested that an enzyme lowers the energy barriers of a reaction by stabilizing preferentially the transition state of the substrate during the reaction rather than the substrate in its ground state.

Linus Carl Pauling Linus Carl Pauling,   American
chemist,   was   known  for
his   works   on   organic
macromolecules   and   on
chemical   links.
 
 
Nobel Price in Chemistry, 1954
Nobel Price for Peace, 1962

           Twenty years later, William Jencks has proposed a strategy to prepare new biocatalysts. This strategy was based on the production of antibodies directed against stable molecules resembling the transition state structure of a specific chemical transformation.

           A breakdown in the field came from the development of the monoclonal antibody technique by Köhler and Milstein that has provided the means for producing antibodies with a single antigenic defined specificity.

           If the first report suggesting that antibodies may act as catalysts was published by the group of Bernard Green, the demonstration that antibodies may be tailor-made to catalyze specifically chemical reactions was simultaneously brought by the Californian laboratories of Richard Lerner and Peter Schultz.

           Since these reports, strategies aimed to improve the efficiency of abzymes were developed, including hapten design, immunization strategies, or methods for screenig and selection (see for review Stevenson and Thomas-2000).






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