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High resolution 'snapshots' detail dynamics of a cocaine antibody

Cocaine-binding antibodies have shown some promise in their ability to neutralize cocaine toxicity, but their binding ability is severely impaired by high concentrations of the drug. A catalytic monoclonal antibody such as 7A1, on the other hand, has the ability to regenerate after each new dose of the drug, making it far more effective than others in metabolizing cocaine.

The study, which will be published in the February issue (Volume 14 Issue 2) of the journal Structure, was led by Ian A. Wilson, D.Phil., of Scripps Research Department of Molecular Biology and The Skaggs Institute for Chemical Biology, and Kim D. Janda, Ph.D., of Scripps Research Departments of Chemistry and Immunology and The Skaggs Institute for Chemical Biology.

Despite intensive research, cocaine abuse continues to be a major public health problem, so far eluding efforts at developing an effective therapeutic agent to counter the craving, addiction, and overdose of the drug. To date, no treatment has been approved by the Food and Drug Administration (FDA).

Commenting on the new findings, Xueyong Zhu, Ph.D., the primary author of the study and a staff scientist in the Wilson laboratory said, "Development of effective therapies for cocaine abuse has been a long-standing goal, and a number of medications under study do show some promise. Immunopharmacotherapy has been proposed as a way to neutralize the drug outside the central nervous system- basically soaking up the drug before it has a chance to cross the blood brain barrier-as a potentially effective new approach to treat cocaine abuse."

Using a monoclonal antibody endowed not only with high binding ability, but also with sufficient catalytic activity to metabolize cocaine, would have potentially enhanced therapeutic effects, Zhu said. This antibody could intercept cocaine in the blood stream before it reaches the central nervous system-stopping the drug cold. Because cocaine has a half life of approximately 30
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Source:Scripps Research Institute


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