Esterase profile and analysis of structure-inhibitor selectivity relationships for homologous phosphorylated 1-hydroperfluoroisopropanols

To characterize the efficiency of interaction of anti-cholinesterase compounds with target esterases, earlier the authors introduced the term the esterase profile of an OPC the set of kinetic constants describing the inhibitory activity of relevant compound with respect to esterases of different functional significance. They showed that the esterase profile is determined by the OPC structure and that it differs for OPCs with different structures. Analysis of the esterase profile of OPCs, especially using modern methods of analysis of the quantitative structure activity relationships (QSAR), makes it possible to determine the contribution of different structural elements to the development and selectivity of a physiological effect. The purpose of this study was to obtain the esterase profile of a series of homologous phosphorylated 1-hydroperuoroisopropanols (PFPs, 4ai) by determining the bimolecular inhibition constants (ki) with respect to AChE, NTE, BChE, and CaE and to analyze the obtained esterase profile by constructing quantitative Hansch models describing the structure inhibitor selectivity.