Increased organophosphate scavenging in a butyrylcholinesterase mutant |
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Authors: | Geyer Brian C Woods Ryan R Mor Tsafrir S |
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Institution: | School of Life Sciences and The Biodesign Institute, P.O. Box 874501, Arizona State University, Tempe, AZ 85287-4501, USA. |
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Abstract: | Nicotiana benthamiana plant lines expressing a reengineered human butyrylcholinesterase (BChE) with enhanced cocaine hydrolase activity were created. Subsequent purification and biochemical analysis revealed that compared to wild-type butyrylcholinesterase, the cocaine hydrolase displayed increased affinity to the organophosphate (OP) pesticides paraoxon (6.84x10(-10)M vs. 1.11x10(-8)M) and malaoxon (9.81x10(-8)M vs. 5.99x10(-7)M). Furthermore, the cocaine hydrolase retained identical anticholinesterase binding profiles for all other compounds tested. Thus we have demonstrated a potential large-scale production platform for a multivalent antidote for cocaine and anticholinesterase poisoning. |
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Keywords: | Bioscavenger Transgenic plants Nerve agents Molecular pharming Cocaine hydrloase Pesticides |
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