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Using phosphorus pentachloride as a substrate, carbacylamidophosphates of the general formula (p‐X‐C6H4) C(O)NHP(O)(R)2; (X=Cl and R=Cl, 2a; X=Br and R=Cl, 3a; X=Me and R=Cl, 4a; X=Cl and R=piperidine, 2b; X=Br and R=piperidine, 3b; X=Me and R=piperidine, 4b; X=H and R=cyclohexylamine, 1c; X=Cl and R=cyclohexylamine, 2c; X=Br and R=cyclohexylamine, 3c; X=Me and R=cyclohexylamine, 4c; X=H and R=p‐Me‐cyclohexylamine, was prepared and characterized by 1H, 31P and 13C NMR and IR spectroscopy and elemental analysis. Different group attached on phosphorus nuclei affect on IR and NMR spectra. Three‐bond coupling constants between phosphorus and carbon nucleus, 3J(P,Caliphatic) in the 1b–4b and 1c–4c containing piperidine or cyclohexylamine groups, were greather than two‐bond coupling constants, 2J(P,Caliphatic). The structures of 2b and 3b were determined by single‐crystal X‐ray diffraction techniques. The both molecule crystals are composed of a centrosymmetric dimer via N‐H···O bonds. 3b exists as two independent molecules in crystal lattice.

Eight newly synthesized carbacylamidophosphates with the general formula RC(O)NHP(O)Cl 2 with RvpClZC 6 H 4 1a, pBrZC 6 H 4 2a, C 6 H 5 3a, and pMeZC 6 H 4 4a and RC(O)NHP(O)(NC 4 H 8 O) 2 RvpClZC 6 H 4 1b, pBrZC 6 H 4 2b, C 6 H 5 3b, pMeZC 6 H 4 4b, were selected to compare the inhibition kinetic parameters, IC 50 , K i , k p and K D , on human erythrocyte acetylcholinesterase (hAChE) and bovine serum butyrylcholinesterase (BuChE), Also, the in vivo inhibition potency of compound 2a, 2b and 3a, were studied. The data demonstrates that compound 2a and compound 2b are the potent sensitive as AChE and BuChE inhibitors respectively, and the inhibition of hAChE is about 10-fold greater than that of BuChE.

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