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Stereoselective Inhibition of Cholesterol Esterase by Enantiomers of exo- and endo-2-Norbornyl-N–n-butylcarbamates

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Abstract

Four stereoisomers of 2-norbornyl-N–n-butylcarbamates are characterized as the pseudo substrate inhibitors of cholesterol esterase. Cholesterol esterase shows enantioselective inhibition for enantiomers of exo- and endo-2-norbornyl-N–n-butylcarbamates. For the inhibitions by (R)-(+)- and (S)-(−)-exo-2-norbornyl-N–n-butylcarbamates, the R-enantiomer is 6.8 times more potent than the S-enantiomer. For the inhibitions by (R)-(+)- and (S)-(−)-endo-2-norbornyl-N–n-butyl-carbamates, the S-enantiomer is 4.6 times more potent than the R-enantiomer. The enzyme-inhibitor complex models have been proposed to explain these different enantioselectivities.

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Abbreviations

ACS:

Acyl chain binding site

CEase:

Cholesterol esterase

LDL:

Low-density lipoprotein

PNPB:

p-nitrophenyl butyrate

TX:

Triton-X 100

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Acknowledgments

We thank the National Science Council of Taiwan for financial support.

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Authors and Affiliations

  1. Department of Internal Medicine, Chung Shan Medical University Hospital, School of Medicine, Chung-Shan Medical University, Taichung, 402, Taiwan

    Ming-Cheng Lin

  2. Department of Chemistry, National Chung-Hsing University, Taichung, 402, Taiwan

    Shyh-Jei Yeh, I-Ru Chen & Gialih Lin

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  1. Ming-Cheng Lin
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  2. Shyh-Jei Yeh
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Correspondence to Gialih Lin.

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Lin, MC., Yeh, SJ., Chen, IR. et al. Stereoselective Inhibition of Cholesterol Esterase by Enantiomers of exo- and endo-2-Norbornyl-N–n-butylcarbamates. Protein J 30, 220–227 (2011). https://doi.org/10.1007/s10930-011-9323-3

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  • DOI: https://doi.org/10.1007/s10930-011-9323-3

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