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- W4295997642 abstract "Sialoglycans play a key role in many biological recognition processes and sialylated conjugates of various types have successfully been applied, e.g., as antivirals or in antitumor therapy. A key feature for high affinity binding of such conjugates is the multivalent presentation of sialoglycans which often possess synthetic challenges. Here, the combination is described of solid phase polymer synthesis and enzymatic sialylation yielding 3′-sialyllactose-presenting precision glycomacromolecules. CMP-Neu5Ac synthetase from Neisseria meningitidis (NmCSS) and sialyltransferase from Pasteurella multocida (PmST1) are combined in a one-pot reaction giving access to sequence-defined sialylated macromolecules. Surprisingly, when employing Tris(hydroxymethyl)aminomethane (Tris) as a buffer, formation of significant amounts of α-linked Tris-sialoside is observed as a side reaction. Further exploring and exploiting this unusual sialylation reaction, different neoglycosidic structures are synthesized showing that PmST1 can be used to derive both, sialylation on natural carbohydrates as well as on synthetic hydroxylated scaffolds." @default.
- W4295997642 created "2022-09-16" @default.
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- W4295997642 date "2022-09-26" @default.
- W4295997642 modified "2023-10-18" @default.
- W4295997642 title "Enzymatic Sialylation of Synthetic Multivalent Scaffolds: From 3′‐Sialyllactose Glycomacromolecules to Novel Neoglycosides" @default.
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- W4295997642 doi "https://doi.org/10.1002/mabi.202200358" @default.
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