| Title : Lipase-catalyzed regioselective monoacetylation of unsymmetrical 1,5-primary diols - Oger_2010_J.Org.Chem_75_1892 |
| Author(s) : Oger C , Marton Z , Brinkmann Y , Bultel-Ponce V , Durand T , Graber M , Galano JM |
| Ref : J Org Chem , 75 :1892 , 2010 |
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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, 2,2'-disubstituted-1,5-pentanediols, and cyclic 2,3-disubstituted-1,5-pentanediols. To rationalize the regioselectivity observed, molecular docking simulations were performed. |
| PubMedSearch : Oger_2010_J.Org.Chem_75_1892 |
| PubMedID: 20187621 |
Oger C, Marton Z, Brinkmann Y, Bultel-Ponce V, Durand T, Graber M, Galano JM (2010)
Lipase-catalyzed regioselective monoacetylation of unsymmetrical 1,5-primary diols
J Org Chem
75 :1892
Oger C, Marton Z, Brinkmann Y, Bultel-Ponce V, Durand T, Graber M, Galano JM (2010)
J Org Chem
75 :1892