Structural and Biochemical Insights into the Inhibition of Human Acetylcholinesterase by G-Series Nerve Agents and Subsequent Reactivation by HI-6.

The recent use of organophosphate nerve agents in Syria, Malaysia, Russia, and the United Kingdom has reinforced the potential threat of their intentional release. These agents act through their ability to inhibit human acetylcholinesterase (hAChE; E.C.

Overcoming the Challenges of Enzyme Evolution To Adapt Phosphotriesterase for V-Agent Decontamination.

The bacterial enzyme phosphotriesterase (PTE) is noted for its ability to hydrolyze many organophosphate compounds, including insecticides and chemical warfare agents. PTE has been the subject of multiple enzyme evolution attempts, which have been highly successful against specific insecticides and the G-type nerve agents. Similar attempts targeting the V-type nerve agents have failed to achieve the same degree of success.

Trace Level Analysis of Sarin and VX in Food Using Normal Phase Silica Gel and Ultra-Performance Liquid Chromatography-Time-of-Flight Mass Spectrometry (UPLC-TOF-MS).

Ultra-Performance Liquid Chromatography/electrospray ionization mass spectrometry was used for the trace level determination of isopropyl methylphosphonofluoridate (Sarin, GB) and ( O-ethyl S-[2-(diisopropylamino)ethyl] methylphosphonothioate (VX) after extraction from various foods. A method utilizing normal phase silica gel was developed for the sample preparation and extraction of VX and GB from food. The extraction efficiencies of the normal phase silica gel method for VX was compared to those of other commercial solid phase extraction media and was found to be comparable.

An OPAA enzyme mutant with increased catalytic efficiency on the nerve agents sarin, soman, and GP.

The wild-type OPAA enzyme has relatively high levels of catalytic activity against several organophosphate G-type nerve agents. A series of mutants containing replacement amino acids at the OPAA Y212, V342, and I215 sites showed several fold enhanced catalytic efficiency on sarin, soman, and GP. One mutant, Y212F/V342L, showed enhanced stereospecificity on sarin and that enzyme along with a phosphotriesterase mutant, GWT, which had the opposite stereospecificity, were used to generate enriched preparations of each sarin enantiomer.

Liquid chromatography-time-of-flight mass spectrometry analysis of 1-(2-chloroethoxy)-2-[(2-chloroethyl)thio] ethane and related compounds: separation of an eleven component mixture.

A method of separation for an eleven component mixture comprised of 1-(2-chloroethoxy)-2-[(2-chloroethyl)thio] ethane (4) and its derivatives has been developed using LC-time-of-flight-MS. All analytical figures of merit for compounds 1-11 have been determined. Compound 4 was examined in a substrate extraction study consisting of different sand and soil matrices, and a hydrolysis study of 4 on sand revealed an extremely complex degradation pathway which appeared to be concentration dependent.