Cyclodextrin-mediated capillary electrophoresis enantioseparation of dansylated beta-amino acids with bicyclo[2.2.2]octane, bicyclo[3.1.1]heptane and cyclopenta[d][1,2]oxazole core structures
The present study investigated the separation of bicyclic beta-amino acids with bicyclo[2.2.2]octane, bicyclo[3.1.1]heptane and cyclopenta[d][1,2]oxazole core structures by capillary electrophoresis using native cyclodextrins as well as neutral and charged derivatives as chiral selectors. The amino...
Elmentve itt :
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| Dokumentumtípus: | Cikk |
| Megjelent: |
2019
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| Sorozat: | ELECTROPHORESIS
40 No. 15 |
| doi: | 10.1002/elps.201800492 |
| mtmt: | 30827972 |
| Online Access: | http://publicatio.bibl.u-szeged.hu/17147 |
| Tartalmi kivonat: | The present study investigated the separation of bicyclic beta-amino acids with bicyclo[2.2.2]octane, bicyclo[3.1.1]heptane and cyclopenta[d][1,2]oxazole core structures by capillary electrophoresis using native cyclodextrins as well as neutral and charged derivatives as chiral selectors. The amino acids were derivatized with dansyl chloride to provide a UV chromophore. Separations were carried out at 20 degrees C in a 48.5/40 cm, 50 mu m fused-silica capillary at an applied voltage of 20 kV. Fifty millimolar sodium phosphate background electrolytes pH 2.5 and 7.2 containing either 5 or 30 mg/mL of the CDs were used. For the majority of the investigated CDs, enantioseparations could only be achieved at pH 2.5 when the analytes are positively charged. Successful enantioseparations as negatively charged analytes at pH 7.2 were only observed for few compounds. In the case of methyl-gamma-cyclodextrin, opposite enantiomer migration order was observed in pH 2.5 or 7.2 background electrolytes. Dependence of the enantiomer migration order on the size of the cavity of the cyclodextrins was also found. Furthermore, the degree of methylation of beta-cyclodextrin derivatives affected the migration order of several analyte enantiomers. |
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| Terjedelem/Fizikai jellemzők: | 1931-1940 |
| ISSN: | 0173-0835 |