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

• Published in: The Journal of Organic Chemistry
• Main Authors: Oger, Camille, Marton, Zsuzsanna, Brinkmann, Yasmin, Bultel-Poncé, Valérie, Durand, Thierry, Graber, Marianne, Galano, Jean-Marie
• Other Authors: Institut des Biomolécules Max Mousseron Pôle Chimie Balard (IBMM), Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie du CNRS (INC)-Université de Montpellier (UM)-Ecole Nationale Supérieure de Chimie de Montpellier (ENSCM), LIttoral ENvironnement et Sociétés - UMRi 7266 (LIENSs), Université de La Rochelle (ULR)-Centre National de la Recherche Scientifique (CNRS)
• Format: Article in Journal/Newspaper
• Language: English
• Published: HAL CCSD 2010
• Subjects: [SDV.BIO]Life Sciences [q-bio]/Biotechnology; [INFO.INFO-BT]Computer Science [cs]/Biotechnology; [CHIM.ORGA]Chemical Sciences/Organic chemistry; Antarc*; Antarctica
• Online Access: https://hal.archives-ouvertes.fr/hal-00647807; https://hal.archives-ouvertes.fr/hal-00647807/document; https://hal.archives-ouvertes.fr/hal-00647807/file/Manuscript_corrige_ressoumis_joc.pdf; https://doi.org/10.1021/jo902541c

International audience 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.