Model studies for enzyme inhibition. Part V: Reactions of organophosphorus compounds with α‐cyclodextrin. A quantitative approach of model activity and stereospecificity
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- 1 January 1972
- journal article
- research article
- Published by Wiley in Recueil des Travaux Chimiques des Pays-Bas
- Vol. 91 (9) , 1103-1109
Abstract
The bimolecular rate constants for reaction of the enantiomers of isopropyl methylphosphonofluoridate, isopropyl p‐nitrophenyl methylphosphonate and isopropyl S‐2‐dimethylaminoethyl methylphosphonothioate with α‐cyclodextrin have been calculated from the dissociation constants (Kdiss) of the prereaction 1:1 inclusion complexes and the maximal rate constants (k2max) for the ensuing nucleophilic reactions. These data are compared with the corresponding rate constants for the inhibition of acetylcholinesterase.It is concluded that the stereospecificity exhibited by α‐cyclodextrin in its reaction with enantiomeric organophosphorus compounds is reflected mainly in the nucleophilic reaction.Keywords
This publication has 7 references indexed in Scilit:
- Über Einschlußverbindungen, XXII. Cyclodextrin‐Imidazol‐VerbindungenEuropean Journal of Inorganic Chemistry, 1970
- Model studies for enzyme inhibition. Part II: The stereospecific reaction of isopropyl p‐nitrophenyl methylphosphonate with α‐cyclodextrin in aqueous alkaline mediaRecueil des Travaux Chimiques des Pays-Bas, 1970
- Stereospecific reaction of isopropyl methylphosphonofluoridate (sarin) with α‐cyclodextrin: A model for enzyme inhibitionRecueil des Travaux Chimiques des Pays-Bas, 1970
- Stereospecificity of hydrolytic enzymes in their reaction with optically active organophosphorus compounds—IIBiochemical Pharmacology, 1967
- ESTER HYDROLYSIS CATALYZED BY α ‐CHYMOTRYPSIN, TRYPSIN AND CYCLODEXTRINS*Transactions of the New York Academy of Sciences, 1967
- The synthesis of optically active isopropyl methylphosphonofluoridate (Sarin): (Preliminary communication)Recueil des Travaux Chimiques des Pays-Bas, 1966
- Stereospecificity of hydrolytic enzymes in their reaction with optically active organophosphorus compounds—I.Biochemical Pharmacology, 1965