Acetylcholinesterase inhibition by two phosphoric 4-nitroanilides

J Enzyme Inhib. 1990;3(3):211-7. doi: 10.3109/14756369009035839.

Abstract

Two phosphoric 4-nitroanilides Z2P(O)NH-phi-NO2 (A, Z = Me; B, Z = NMe2) have been prepared and purified by chromatographic techniques. Their spectral data (uv, ir and 1H-nmr) have been determined, and compared with those of other similar compounds. Their ability to inhibit acetylcholinesterase has been measured by a modification of Ellman's method. The data, as computed according to the Michaelis scheme, indicate that A is not an inhibitor, whereas B is a reversible mixed one. These differences are discussed in terms of hydrophobic interactions.

MeSH terms

  • Acetylcholinesterase / metabolism
  • Anilides / chemical synthesis*
  • Anilides / isolation & purification
  • Anilides / pharmacology
  • Animals
  • Cholinesterase Inhibitors / chemical synthesis*
  • Chromatography, High Pressure Liquid
  • Chromatography, Thin Layer
  • Electrophorus
  • Indicators and Reagents
  • Kinetics
  • Magnetic Resonance Spectroscopy
  • Organophosphorus Compounds / chemical synthesis*
  • Organophosphorus Compounds / isolation & purification
  • Organophosphorus Compounds / pharmacology
  • Spectrophotometry
  • Structure-Activity Relationship

Substances

  • Anilides
  • Cholinesterase Inhibitors
  • Indicators and Reagents
  • Organophosphorus Compounds
  • N-(4-nitrophenyl)dimethylphosphinamide
  • N,N,N',N'-tetramethyl-N''-(4-nitrophenyl)phosphoric triamide
  • Acetylcholinesterase