Acetylcholinesterase inhibition by two phosphoric 4-nitroanilides

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...

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Bibliographic Details
Published in:	Journal of enzyme inhibition Vol. 3; no. 3; p. 211
Main Authors:	Bollinger, J C, Levy-Serpier, J, Debord, J, Penicaut, B
Format:	Journal Article
Language:	English
Published:	Switzerland 1990
Subjects:	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
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Summary:	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.
ISSN:	8755-5093
DOI:	10.3109/14756369009035839