Reactions of VX, GB, GD, and HD with nanosize Al(2)O(3). Formation of aluminophosphonates.

Room-temperature reactions of VX, GB, GD, and HD with nanosize Al(2)O(3) (AP-Al(2)O(3)) have been characterized by (31)P, (13)C, and (27)Al MAS NMR. Nerve agents VX, GB, and GD hydrolyze to yield surface-bound complexes of their corresponding nontoxic phosphonates. At sufficiently high loadings, discreet aluminophosphonate complexes, Al[OP(O)(CH(3))OR](3), are generated which are identical to synthesized model compounds.

Synthesis and anticholinesterase activity of new bispyridinium compounds.

Synthesis of new bis(1-methylpyridinium) compounds containing a 1,4-diacetylbenzene linkage between the pyridinium moieties from commercially available 2-, 3-, and 4-picoline precursors was accomplished via metallation, reaction of the picolyllithium with 1,4-dicyanobenzene, and subsequent quaternization of the resulting bispyridyl compounds. Acetylcholinesterase inhibitory activity was determined colorimetrically with purified electric eel enzyme. Examination of structure-activity relationships indicated that the 3-substituted pyridinium compound is the most potent isomer, followed by the 2-substituted isomer, and that the 4-substituted analogue is the least active.

O-demethylation of pyrilamine.

O-Demethylation of pyrilamine with l-propanethiol and potassium tert-butoxide gave hydroxytripelennamine, one of the major metabolites of tripelennamine. The reaction of pyrilamine with other demethylating agents has been explored and the products formed have been characterized. The reaction of pyrilamine with 48% hydrobromic acid yielded 2-(2-dimethylaminoethyl)aminopyridine.

Thin-layer chromatography of mustard and its metabolites.

Since its recently alleged use in the Middle East armed conflict, the chemical agent mustard has been in the news. Exposure to mustard causes extremely painful physiological manifestations. On entering the biological system, it is metabolized and converted into various products.

Identification of NADPH-thioredoxin reductase system in Euglena gracillis.

Euglena gracilis contains a protein system which can utilize the reducing power of NADPH in the ribonucleotide reductase-catalyzed reduction of CTP. The proteins required for this reaction are a flavoprotien with a molecular weight of approximately 185,000 which is functionally similar to thioredoxin reductase (NADPH), EC 1.6.