Related Experiment Video
Updated: Jul 2, 2026

Quantifying the Modulation of Elastase Enzyme Activity Through Colorimetric Analysis
Published on: January 17, 2025
Synthesis and elastase-inhibiting activity of 2-pyridinyl-isothiazol-3(2H)-one 1,1-dioxides
Alexander Eilfeld1, Camino M González Tanarro, Maxim Frizler
1Institute for Organic Chemistry, University of Leipzig, Johannisallee 29, D-04103 Leipzig, Germany.
Abstract:
The synthesis of a series of new isothiazol-3(2H)-one 1,1-dioxides with halogenated (mostly fluorinated) pyridinyl and pentafluorophenyl substituents at 2-position is reported. These compounds (18-24) became easily accessible from 2-thiocyanato-1-carboxaldehydes and aminopyridines, pentafluoroaniline, respectively, by an isothiazolium cyclization-oxidation route. Compound 21 exhibited an IC(50) value of 3.1 microM toward human leukocyte elastase. The proteases cathepsin G, trypsin, cathepsin L, and angiotensin-converting enzyme, and the serine esterases acetylcholinesterase and cholesterol esterase were not inhibited by 21.
More Related Videos
Related Concept Videos
Oxidation of Alkenes: Syn Dihydroxylation with Osmium Tetraoxide
Inhibitors of Bacterial DNA Synthesis
ortho–para-Directing Activators: –CH3, –OH, –⁠NH2, –OCH3
Enzyme Inhibition

