| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 5280320 | Tetrahedron Letters | 2007 | 4 Pages |
α-Chymotrypsin catalyzed peptide bond formation was studied in ionic liquids using the synthesis of a protected fragment of Leu-enkephalin, ZTyrGlyGlyOEt, as model reaction. MOEMIM·PF6 was found to be the most favorable solvent among the six different 1-alkyl-3-methylimidazolium hexafluorophosphates and tetrafluoroborates ionic liquids screened. With MOEMIM·PF6 as reaction media, several di- or tripeptide derivatives were successfully prepared in 68-75% isolated yields.
Graphical abstractα-Chymotrypsin catalyzed peptide bond formation was studied in ionic liquids using the synthesis of a protected fragment of Leu-enkephalin, ZTyrGlyGlyOEt, as model reaction. MOEMIM·PF6 was found to be the most favorable solvent among the six different 1-alkyl-3-methylimidazolium hexafluorophosphates and tetrafluoroborates ionic liquids screened. With MOEMIM·PF6 as reaction media, several di- or tripeptide derivatives were successfully prepared in 68-75% isolated yields.Download full-size image
