Lipase-catalyzed regioselective monoacetylation of unsymmetrical 1,5-primary diols.
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, 2,2'-disubstituted-1,5-pentanediols, and cyclic 2,3-disubstituted-1,5-pentanediols. To rationalize the regioselectivity observed, molecular docking simulations were performed.
Oger
Camille
C
Institut des Biomolécules Max Mousseron, UMR 5247 CNRS, Université Montpellier I, Faculté de Pharmacie, 15 avenue Charles Flahault, BP 14491, 34093 Montpellier, Cedex 05, France.
Marton
Zsuzsanna
Z
Brinkmann
Yasmin
Y
Bultel-Poncé
Valérie
V
Durand
Thierry
T
Graber
Marianne
M
Galano
Jean-Marie
JM
D000107:Acetylation; D002175:Candida / Q000201:enzymology; D002384:Catalysis; D003198:Computer Simulation; D006900:Hydroxylation; D028421:Isoprostanes / Q000737:chemistry; D008049:Lipase / Q000737:chemistry*; D008958:Models, Molecular; D015394:Molecular Structure; D013237:Stereoisomerism
D028421:Isoprostanes; D008049:Lipase