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|標題:||Stereoselective inhibition of butyrylcholinesterase by enantiomers of exo- and endo-2-norbornyl-N-n-butylcarbamates||作者:||Chiou, S.Y.
|關鍵字:||Butyrylcholinesterase;carbamate inhibitor;enantiomer;stereoselectivity;resolution by lipase;cholesterol esterase;alzheimers-disease;acetylcholinesterase;inhibition;molecular recognition;crystal-structure;highly potent;cholinesterases;mechanism;hydrolysis;site||Project:||Journal of Enzyme Inhibition and Medicinal Chemistry||期刊/報告no：:||Journal of Enzyme Inhibition and Medicinal Chemistry, Volume 25, Issue 1, Page(s) 13-20.||摘要:||
Enantiomers of exo- and endo-2-norbornyl-N-n-butylcarbamates were characterized as pseudo substrate inhibitors of butyrylcholinesterase. These inhibitions discriminate enantiomers of the inhibitors and therefore show stereoselectivity for the enzyme. For inhibitions by (R)-(+)- and (S)-(-)-exo-2-norbornyl-N-n-butylcarbamates, R-enantiomer is a more potent inhibitor than S-enantiomer. But, for inhibitions by (R)-(+)- and (S)-(-)-endo-2-norbornyl-N-n-butylcarbamates, S-enantiomer is a more potent inhibitor than R-enantiomer. Optically pure (R)-(+)-exo-, (S)-(-)-exo-, (R)-(+)-endo-, and (S)-(-)-endo-2-norbornyl-N-n-butylcarbamates were synthesized from condensations of optically pure (R)-(+)-exo-, (S)-(-)-exo-, (R)-(+)-endo-, and (S)-(-)-endo-2-norborneols with n-butyl isocyanate, respectively. Optically pure norborneols were obtained from kinetic resolution of their racemic esters by lipase catalysis in organic solvent.
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