Nerve agent and toxic pesticide neutralizer

Catalytic efficiency of this mutant enzyme is approximately 4 times greater than the wild-type enzyme and may be the only compound effective against EA 1356

Medical & Biotechnology Military Technology Environmental

Army researchers have identified enzyme mutations that can neutralize a toxic compound used in chemical weapons and pesticides. Businesses can use the new technology to create products or services by licensing the patent.

Students test a dummy for contamination inside the Chemical Defense Training Facility at Fort Leonard Wood, Missouri. (Army photo)

A number of organophosphorus (OP) compounds used by the agriculture industry and the military are highly toxic and thus hazardous to human health and harmful to the environment.

For example, acetylcholinesterase-inhibiting OP compounds comprise the active ingredient of pesticides such as paraoxon as well as G-type nerve agents such as sarin and soman, and V-type nerve agents developed for chemical warfare. Thus, it is very important to be able to detoxify such OP compounds and to decontaminate surfaces and substances exposed to these compounds.

One approach being investigated as a potential solution to this problem is enzyme-mediated decontamination.

For example, a class of enzymes known as organophosphorus acid anhydrolases (OPAA) can catalyze the hydrolysis of a variety of OP compounds, including pesticides and fluorinated G-type nerve agents. These anhydrolases can be mass produced in cell culture systems.

One of the OP compounds in particular, 2-methylcyclohexyl methylphosphonofluoridate, known as EA 1356, is very toxic to humans. A native OPAA enzyme has previously been discovered to possess catalytic activity against this compound but greater catalytic efficiencies are needed. No efficient and easily produced catalyst for EA 1356 degradation in the environment or in vivo is known.

Starting with the wild type OPAA enzyme, Army researchers have identified three mutations in the enzyme which deliver greatly enhanced catalytic activity against EA 1356. The catalytic efficiency of this mutant on EA 1356 is approximately 4 times greater than the wild-type enzyme and may have the highest value ever reported for an enzyme active on EA 1356.

This non-wild-type OPAA may be provided for pharmaceutical use and delivered to a subject by injection with a pharmaceutically acceptable carrier. The enzyme could also be used in a solution to wipe down contaminated surfaces.

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