Lipase-catalyzed regioselective monoacetylation of unsymmetrical 1,5-primary diolsReportar como inadecuado




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* Corresponding author 1 UMR 5247 CNRS 2 LIENSs - LIttoral ENvironnement et Sociétés - UMR 7266 3 IBMM - Institut des Biomolécules Max Mousseron Pôle Chimie Balard

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.





Autor: Camille Oger - Zsuzsanna Marton - Yasmin Brinkmann - Valérie Bultel-Poncé - Thierry Durand - Marianne Graber - Jean-Marie Galan

Fuente: https://hal.archives-ouvertes.fr/



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