1219451-18-9Relevant academic research and scientific papers
Inhibition of acetylcholinesterase by chromophore-linked fluorophosphonates
Guo, Lilu,Suarez, Alirica I.,Braden, Michael R.,Gerdes, John M.,Thompson, Charles M.
scheme or table, p. 1194 - 1197 (2010/06/15)
Fluorophosphonate (FP) head groups were tethered to a variety of chromophores (C) via a triazole group and tested as FPC inhibitors of recombinant mouse (rMoAChE) and electric eel (EEAChE) acetylcholinesterase. The inhibitors showed bimolecular inhibition constants (ki) ranging from 0.3 × 105 M-1 min-1 to 10.4 × 105 M-1 min-1. When tested against rMoAChE, the dansyl FPC was 12.5-fold more potent than the corresponding inhibitor bearing a Texas Red as chromophore, whereas the Lissamine and dabsyl chromophores led to better anti-EEAChE inhibitors. Most inhibitors were equal or better inhibitors of rMoAChE than EEAChE. 3-Azidopropyl fluorophosphonate, which served as one of the FP head groups, showed excellent inhibitory potency against both AChE's (? 1 × 107 M-1 min-1) indicating, in general, that addition of the chromophore reduced the overall anti-AChE activity. Covalent attachment of the dabsyl-FPC analog to rMoAChE was demonstrated using size exclusion chromatography and spectroscopic analysis, and visualized using molecular modeling.
