A versatile approach to optically active primary 2-fluoro-2-phenylalkanols through lipase-catalyzed transformations

Kinetic resolutions of (+/-)-1-acetoxy-2-fluoro-2-phenylalkanes 1 by enzymatic hydrolysis and of (+/-)-2-fluoro-2-phenylpropanol 2a by lipase-catalyzed acetylation are described for the first time. Hydrolysis of (+/-)-1 with lipase Amano PS (Pseudomonas cepacia) provided both the optically active acetates (-)-1 and the corresponding primary alcohols (-)-2 with high enantiomeric excess. (R)-enantiopreference was observed for the acetylation of (+/-)-2-fluoro-2-phenylpropanol 2a which occurred with higher enantioselectivity and faster conversion compared to the unfluorinated parent compound (+/-)-2-phenylpropanol 3. (C) 1997 Elsevier Science Ltd. All rights reserved.