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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2011
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| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_10242422_v29_n2-3_p87_Monsalve http://hdl.handle.net/20.500.12110/paper_10242422_v29_n2-3_p87_Monsalve |
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paper:paper_10242422_v29_n2-3_p87_Monsalve2023-06-08T16:00:13Z Biocatalytic synthesis of chiral N-(2-hydroxyalkyl)-acrylamides Candida antarctica lipase B Mosher' s method N-(hydroxyalkyl)-acrylamides primary alcohol stereoselectivity Enantiomers Absolute stereochemistry Acrylamides Biocatalytic synthesis Candida antarctica lipase B Enantiomeric excess Lipase-catalyzed resolution Mosher' s method Primary alcohols Stereoselectivity 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 Candida antarctica 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. 2011 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_10242422_v29_n2-3_p87_Monsalve http://hdl.handle.net/20.500.12110/paper_10242422_v29_n2-3_p87_Monsalve |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
Candida antarctica lipase B Mosher' s method N-(hydroxyalkyl)-acrylamides primary alcohol stereoselectivity Enantiomers Absolute stereochemistry Acrylamides Biocatalytic synthesis Candida antarctica lipase B Enantiomeric excess Lipase-catalyzed resolution Mosher' s method Primary alcohols Stereoselectivity 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 Candida antarctica |
| spellingShingle |
Candida antarctica lipase B Mosher' s method N-(hydroxyalkyl)-acrylamides primary alcohol stereoselectivity Enantiomers Absolute stereochemistry Acrylamides Biocatalytic synthesis Candida antarctica lipase B Enantiomeric excess Lipase-catalyzed resolution Mosher' s method Primary alcohols Stereoselectivity 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 Candida antarctica Biocatalytic synthesis of chiral N-(2-hydroxyalkyl)-acrylamides |
| topic_facet |
Candida antarctica lipase B Mosher' s method N-(hydroxyalkyl)-acrylamides primary alcohol stereoselectivity Enantiomers Absolute stereochemistry Acrylamides Biocatalytic synthesis Candida antarctica lipase B Enantiomeric excess Lipase-catalyzed resolution Mosher' s method Primary alcohols Stereoselectivity 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 Candida antarctica |
| description |
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. |
| title |
Biocatalytic synthesis of chiral N-(2-hydroxyalkyl)-acrylamides |
| title_short |
Biocatalytic synthesis of chiral N-(2-hydroxyalkyl)-acrylamides |
| title_full |
Biocatalytic synthesis of chiral N-(2-hydroxyalkyl)-acrylamides |
| title_fullStr |
Biocatalytic synthesis of chiral N-(2-hydroxyalkyl)-acrylamides |
| title_full_unstemmed |
Biocatalytic synthesis of chiral N-(2-hydroxyalkyl)-acrylamides |
| title_sort |
biocatalytic synthesis of chiral n-(2-hydroxyalkyl)-acrylamides |
| publishDate |
2011 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_10242422_v29_n2-3_p87_Monsalve http://hdl.handle.net/20.500.12110/paper_10242422_v29_n2-3_p87_Monsalve |
| _version_ |
1768542230533898240 |