Hydrolase-mediated resolution of the hemiacetal in 2-chromanols: The impact of remote substitution |
| |
| Authors: | Declan P. Gavin,Aoife Foley,Thomas S. Moody,U.B. Rao Khandavilli,Simon E. Lawrence,Pat O&#x Neill,Anita R. Maguire |
| |
| Affiliation: | 1. Department of Chemistry, Analytical & Biological Research Facility, Synthesis and Solid State Pharmaceutical Centre, University College Cork, Cork, Ireland;2. Almac, Department of Biocatalysis & Isotope Chemistry, 20 Seagoe Industrial Estate, Craigavon, BT63 5QD N. Ireland, UK;3. Pfizer Global Process Development Centre, Loughbeg, Co., Cork, Ireland;4. Department of Chemistry and School of Pharmacy, Analytical & Biological Research Facility, Synthesis and Solid State Pharmaceutical Centre, University College Cork, Cork, Ireland |
| |
| Abstract: | Hydrolase-catalysed dynamic kinetic resolutions of chroman-2-ol and 3-methyl chroman-2-ol can be effected with up to 88% conversion and 92% ee through the use of organic solvents. Extension to the resolution of the tolterodine precursor 1 proved more challenging. The presence of the remote phenyl substituent had a significant impact on the resolution and it was not possible to achieve high enantioselectivity together with efficient conversion from the focussed panel of enzymes screened. |
| |
| Keywords: | Corresponding author. |
| 本文献已被 ScienceDirect 等数据库收录！ |
|
