| Autor: |
Joana Silva, Reynard Spiess, Andrea Marchesi, Sabine L. Flitsch, Julie E. Gough, Simon J. Webb |
| Rok vydání: |
2022 |
| Předmět: |
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| Zdroj: |
Silva, J, Spiess, R, Marchesi, A, Flitsch, S L, Gough, J & Webb, S 2022, ' Enzymatic elaboration of oxime-linked glycoconjugates in solution and on liposomes ', Journal of Materials Chemistry B . https://doi.org/10.1039/D2TB00714B |
| ISSN: |
2050-7518 |
| Popis: |
Oxime formation is a convenient one-step method for ligating reducing sugars to surfaces, producing a mixture of closed ring α- and β-anomers along with open-chain (E)- and (Z)-isomers. Here we show that despite existing as a mixture of isomers, N-acetylglucosamine (GlcNAc) oximes can still be substrates for β(1,4)-galactosyltransferase (β4GalT1). β4GalT1 catalysed the galactosylation of GlcNAc oximes by a galactose donor (UDP-Gal) both in solution and in situ on the surface of liposomes, with conversions up to 60% in solution and ca. 15-20% at the liposome surface. It is proposed that the β-anomer is consumed preferentially but long reaction times allow this isomer to be replenished by equilibration from the remaining isomers. Adding further enzymes gave more complex oligosaccharides, with a combination of α-1,3-fucosyltransferase, β4GalT1 and the corresponding sugar donors providing Lewis X coated liposomes. However, sialylation using T. cruzi trans-sialidase and sialyllactose provided only very small amounts of sialyl Lewis X (sLex) capped lipid. These observations show that combining oxime formation with enzymatic elaboration will be a useful method for the high-throughput surface modification of drug delivery vehicles, such as liposomes, with cell-targeting oligosaccharides. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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