Novel chemoenzymatic strategy for the synthesis of enantiomerically pure secondary alcohols with sterically similar substituents

• Published in: The Journal of Organic Chemistry
• Main Authors: Abad, José Luis, Soldevila, Carles, Camps Díez, Francisco, Clapés Saborit, Pere
• Format: Article in Journal/Newspaper
• Language: English
• Published: American Chemical Society 2003
• Subjects: Chemoenzymatic methodology; Secondary alcohols; Enzymatic resolution; Sex pheromone biosynthesis; Antarc*; Antarctica
• Online Access: http://hdl.handle.net/10261/20227; https://doi.org/10.1021/jo0341113

6 pages, 2 figures, 1 scheme, 2 tables.-- PMID: 12816498 [PubMed].-- Printed version published Jun 27, 2003.-- Supporting information available at: http://pubs.acs.org/doi/suppl/10.1021/jo0341113 A novel chemoenzymatic strategy for the synthesis of enantiomerically pure secondary alcohols with sterically similar substituents is described. The key step is the kinetic lipase-catalyzed resolution of racemic mixtures of substituted propargylic alcohols. The efficiency of this new approach was tested in the preparation of the corresponding enantiomers of 1,11-hexadecandiol derivatives ((R)-5 and (S)-5). Two strategies were tested. In the first one, the racemic intermediate 1-octyn-3-ol (1) was resolved enzymatically and then elongated with 1-bromo-9,11-dioxadodecane. Alternatively, the racemic 1 can be elongated to the corresponding racemic 17,19-dioxa-7-eicosyn-6-ol (3) first and then resolved biocatalytically. Twelve commercially available lipases were screened for the kinetic resolution of these intermediates. Among them, Candida antarctica lipase (CAL-B) and Humicola lanuginosa lipase (HLL) were the best biocatalysts for the resolution of 1 (S enantiomer 90% ee, E = 35), and 3 (R enantiomer 90% ee, E = 34), respectively. CICYT and FEDER (AGL2001-0585) and Generalitat de Catalunya (2001SGR 00342). Peer reviewed