Lipase-catalyzed regioselective monoacetylation of unsymmetrical 1,5-primary diols - Archive ouverte HAL Access content directly
Journal Articles Journal of Organic Chemistry Year : 2010

Lipase-catalyzed regioselective monoacetylation of unsymmetrical 1,5-primary diols

Abstract

Lipase B from Candida antarctica (CALB) has been selected as the most suitable enzyme to catalyze the regioselective monoacetylation of 1,5-diol isoprostane intermediate, using vinyl acetate as an acyl transfer reagent in THF.We next applied this reaction on linear 2-substituted, 2,20-disubstituted-1,5- pentanediols, and cyclic 2,3-disubstituted-1,5-pentanediols. To rationalize the regioselectivity observed, molecular docking simulations were performed.
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Dates and versions

hal-00647807 , version 1 (02-12-2011)

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Camille Oger, Zsuzsanna Marton, Yasmin Brinkmann, Valérie Bultel-Poncé, Thierry Durand, et al.. Lipase-catalyzed regioselective monoacetylation of unsymmetrical 1,5-primary diols. Journal of Organic Chemistry, 2010, 75, pp.1892-1897. ⟨10.1021/jo902541c⟩. ⟨hal-00647807⟩
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