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

Camille Oger (1) , Zsuzsanna Marton (2) , Yasmin Brinkmann (1) , Valérie Bultel-Poncé (1) , Thierry Durand (1) , Marianne Graber (2) , Jean-Marie Galano (1)

1 IBMM - Institut des Biomolécules Max Mousseron [Pôle Chimie Balard]
2 LIENSs - LIttoral ENvironnement et Sociétés

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.

Domaines: Biotechnologies; Biotechnologie; Chimie organique

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⟩