MINI-REVIEW: Creation of Catalytic Antibodies Metabolizing Organophosphate Compounds

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I. N. Kurkova, I. V. Smirnov, A. A. Belogurov, Jr., N. A. Ponomarenko, and A. G. Gabibov^*

Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, ul. Miklukho-Maklaya 16/10, 117997 Moscow, Russia; fax: (495) 330-6983; E-mail: kurkova.inna@gmail.com; smirnov@mx.ibch.ru; belogurov@mx.ibch.ru; natalie@mx.ibch.ru; gabibov@mx.ibch.ru

^* To whom correspondence should be addressed.

Received June 22, 2012; Revision received July 2, 2012

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Development of new ways of creating catalytic antibodies possessing defined substrate specificity towards artificial substrates has important fundamental and practical aspects. Low immunogenicity combined with high stability of immunoglobulins in the blood stream makes abzymes potent remedies. A good example is the cocaine-hydrolyzing antibody that has successfully passed clinical trials. Creation of an effective antidote against organophosphate compounds, which are very toxic substances, is a very realistic goal. The most promising antidotes are based on cholinesterases. These antidotes are now expensive, and their production methods are inefficient. Recombinant antibodies are widely applied in clinics and have some advantage compared to enzymatic drugs. A new potential abzyme antidote will combine effective catalysis comparable to enzymes with high stability and the ability to switch on effector mechanisms specific for antibodies. Examples of abzymes metabolizing organophosphate substrates are discussed in this review.

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KEY WORDS: catalytic antibodies, abzymes, organophosphate compounds, biocatalysis

DOI: 10.1134/S0006297912100069

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