Biocatalytic synthesis of chiral N-(2-hydroxyalkyl)-acrylamides

The preparation of a series of novel chiral N-(2-hydroxylalkyl)-acrylamides through a lipase-catalyzed resolution of racemic alkanolamines is described. The absolute stereochemistry and enantiomeric excess of the products were determined by a modified Mosher's method. The method was validated f...

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Bibliographic Details
Main Authors: Monsalve, L.N., Rustoy, E.M., Baldessari, A.
Format: Journal/Newspaper
Language:unknown
Subjects:
Candida antarctica lipase B
Mosher' s method
N-(hydroxyalkyl)-acrylamides
primary alcohol
stereoselectivity
Enantiomers
Absolute stereochemistry
Acrylamides
Biocatalytic synthesis
Enantiomeric excess
Lipase-catalyzed resolution
Primary alcohols
acrylamide derivative
alkanolamine
triacylglycerol lipase
aminolysis
article
biocatalysis
Candida antarctica
catalyst
chemical reaction
chirality
enantiomer
enantioselectivity
enzyme mechanism
enzyme specificity
Mosher method
nonhuman
reliability
stereochemistry
structure analysis
synthesis
technique
Antarc*
Antarctica
Online Access:https://hdl.handle.net/20.500.12110/paper_10242422_v29_n2-3_p87_Monsalve
Description
Summary:The preparation of a series of novel chiral N-(2-hydroxylalkyl)-acrylamides through a lipase-catalyzed resolution of racemic alkanolamines is described. The absolute stereochemistry and enantiomeric excess of the products were determined by a modified Mosher's method. The method was validated for this particular case by the synthesis of an enantiomerically pure product. Moreover, the stereoselective behavior of the lipase in this reaction is discussed. © 2011 Informa UK, Ltd.

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