While(13)C-labelled proteins are common tools in NMR studies, lack of access to(13)C-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-C-13(6)]-Fuc labelled type I Lewis b (Le(b)) structures have been synthesised for use in NMR binding studies with the Blood-group Antigen Binding Adhesin (BabA), a membrane-bound protein from the bacteriumHelicobacter pylori. As part of this work, an efficient synthesis of a benzylatedl-[U-C-13(6)]-Fuc thioglycoside donor froml-[U-C-13(6)]-Gal has been developed. The design and synthesis of an orthogonally protected tetrasaccharide precursor enabled controlled introduction of one or two(13)C-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.