Synthesis of Type 1 Lewis b hexasaccharide antigen structures featuring flexible incorporation of L-[U-13C6]-fucose for NMR binding studies
Allbwn ymchwil: Cyfraniad at gyfnodolyn › Erthygl › adolygiad gan gymheiriaid
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Yn: Organic and Biomolecular Chemistry, Cyfrol 18, Rhif 23, 21.06.2020, t. 4452-4458.
Allbwn ymchwil: Cyfraniad at gyfnodolyn › Erthygl › adolygiad gan gymheiriaid
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T1 - Synthesis of Type 1 Lewis b hexasaccharide antigen structures featuring flexible incorporation of L-[U-13C6]-fucose for NMR binding studies
AU - Long, Mark
AU - Ni Cheallaigh, Aisling
AU - Reihill, Mark
AU - Oscarson, Stefan
AU - Lahmann, Martina
PY - 2020/6/21
Y1 - 2020/6/21
N2 - 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
AB - 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
U2 - 10.1039/D0OB00426J
DO - 10.1039/D0OB00426J
M3 - Article
VL - 18
SP - 4452
EP - 4458
JO - Organic and Biomolecular Chemistry
JF - Organic and Biomolecular Chemistry
SN - 1477-0520
IS - 23
ER -