| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 69608 | Journal of Molecular Catalysis B: Enzymatic | 2013 | 7 Pages |
•Sugar and lipid modified enkephalin peptides were chemically synthesized.•LgtC galactosyltransferase catalyzed conversion of enkephalin derivatives.•Galactosylated products were purified in 13–71% yields.•5% DMSO increased solubility and enzymatic conversion of lipidated enkephalins.•LgtC displayed unexpectedly high substrate specificity toward galactosyl moieties.
Glycosylation of therapeutic peptides has been reported to improve delivery and targeting of various vaccines and drugs to specific cells/tissues. However, chemical synthesis of complex oligosaccharide derivatives via conventional methods can be challenging due to the need for several orthogonal hydroxyl group protections. Liposaccharyl galactosyltransferase C, a naturally occurring glycosyltransferase enzyme from Neisseria meningitidis, was found to have the ability to transfer a galactosyl moiety to glyco(lipo)peptides. An enzymatic glycosylation of Leu-enkephalin glyco(lipo)peptides was developed and optimized in this study in order to prepare pain regulating peptides with potentially improved central nervous system delivery.
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