Synthesis of Type 1 Lewis b hexasaccharide antigen structures featuring flexible incorporation of L-[U-13C6]-fucose for NMR binding studies
Research output: Contribution to journal › Article › peer-review
Electronic versions
Documents
- 13C-Lewis-OBC-accepted manuscript-D0OB00426J
Accepted author manuscript, 1.55 MB, PDF document
DOI
While 13C-labelled proteins are common tools in NMR studies, lack of access to 13C-labelled carbohydrate structures has restricted their use. L-fucose is involved in a wide range of physiological and pathophysiological processes in mammalian organisms. Here, L-[U-13C6]-Fuc labelled type I Lewis b (Leb) structures have been synthesised for use in NMR binding studies with the Blood-group Antigen Binding Adhesin (BabA), a membrane-bound protein from the bacterium Helicobacter pylori. As part of this work, an efficient synthesis of a benzylated L-[U-13C6]-Fuc thioglycoside donor from L-[U-13C6]-Gal has been developed. The design and synthesis of an orthogonally protected tetrasaccharide precursor enabled controlled introduction of one or two 13C-labelled or non-labelled fucosyl residues prior to global deprotection. NMR analysis showed that it is straightforward to assign the anomeric centres as well as the H-5 positions to the individual fucosyl residues which are relevant for NMR binding studies
Original language | English |
---|---|
Pages (from-to) | 4452-4458 |
Journal | Organic and Biomolecular Chemistry |
Volume | 18 |
Issue number | 23 |
DOIs | |
Publication status | Published - 21 Jun 2020 |
Total downloads
No data available