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• W4283204633 abstract "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." @default.
• W4283204633 created "2022-06-22" @default.
• W4283204633 creator A5013506078 @default.
• W4283204633 creator A5028515943 @default.
• W4283204633 creator A5049687470 @default.
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• W4283204633 creator A5082813286 @default.
• W4283204633 creator A5090461916 @default.
• W4283204633 date "2022-01-01" @default.
• W4283204633 modified "2023-10-15" @default.
• W4283204633 title "Enzymatic elaboration of oxime-linked glycoconjugates in solution and on liposomes" @default.
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• W4283204633 doi "https://doi.org/10.1039/d2tb00714b" @default.
• W4283204633 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/35723603" @default.

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