Photolysis of chlorantraniliprole and cyantraniliprole in water and soil: verification of degradation pathways via kinetics modeling.

Photodegradation of [(14)C]-chlorantraniliprole (CLAP) and [(14)C]-cyantraniliprole (CNAP) was investigated in sterile buffer solutions, in natural water, and on soil surfaces. Both compounds displayed rapid degradation in aqueous buffers when exposed to light at concentrations which could result from direct overspray to a shallow water body. While the main products observed had analogous structures, a substantial difference was noted in the rate of degradation of the two compounds despite minimal differences in their structures.

Hydrolysis of chlorantraniliprole and cyantraniliprole in various pH buffer solutions.

The hydrolysis reactions of [(14)C]-chlorantraniliprole (CLAP) and cyantraniliprole (CNAP) were investigated in sterile buffer solutions at pH 4, 7, and 9. Both compounds displayed similar degradation reactions. The reactions observed were intramolecular cyclizations and rearrangements instead of the anticipated amide hydrolysis to carboxylic acids.

Pyrolysis of [14C]-chlorantraniliprole in tobacco.

The pyrolysis of [(14)C]-chlorantraniliprole {3-bromo-1-(3-chloro-2-pyridinal)-N-[4-chloro-2-methyl-6-[(methylamino)carbonyl]phenyl]-1H-pyrazole-5-carboxamide} in tobacco was examined. Typically five commercially available cigarettes were treated separately with either [pyrazole carbonyl-(14)C] or [benzamide carbonyl-(14)C]-chlorantraniliprole at a concentration of 20 ppm (μg chlorantraniliprole equivalent/g cigarette weight; main study) to 40 ppm (for degradate identification only). All treated cigarettes were smoked using an apparatus designed to collect mainstream (MS) and sidestream (SS) smoke through a glass fiber filter and a series of liquid traps.

The Bogorol family of antibiotics: template-based structure elucidation and a new approach to positioning enantiomeric pairs of amino acids.

The sequence positions of d and l Leu and Lys residues in bogorol A (1) have been defined by a simple and novel approach that utilizes small amounts of sample and focuses on detecting the order in which amino acids are liberated from the parent peptide during acid-catalyzed hydrolysis. This technique builds on a previously established relationship between the steric and electronic features of amino acids and their predilection for acidic liberation from polypeptides via dipeptides. The results, which complete the structure of bogorol A, have been confirmed by traditional degradation experiments.