Studies on the interactions between glycosylated beta3-peptides and the lectin Vicia villosa by saturation transfer difference NMR spectroscopy.
Saturation transfer difference (STD) NMR spectroscopy was used to study the interaction of the lectin Vicia villosa (VVLB(4)) with alpha-D-GalNAc glycosylated beta(3)-peptides. The data were compared to those obtained with the monosaccharides D-Gal, D-GalNAc, and D-Glc as well as with those obtained with the Tn antigen alpha-glycopeptide (D-GalNAc-alpha-O-Ser/Thr), molecule naturally recognized by V. villosa. Evidence that the lectin also recognizes glycosylated beta(3)-peptides and has close contact with both the sugar and amino acid moieties was obtained.
Kaszowska
Marta
M
Department of Chemistry, Swedish University of Agricultural Sciences, PO Box 7015, SE-750 07 Uppsala, Sweden.
Norgren
Anna S
AS
Arvidson
Per I
PI
Sandström
Corine
C
D015295:Antigens, Tumor-Associated, Carbohydrate; D006020:Glycopeptides / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D008968:Molecular Conformation; D009005:Monosaccharides; D037121:Plant Lectins / Q000737:chemistry*; D011485:Protein Binding
D015295:Antigens, Tumor-Associated, Carbohydrate; D006020:Glycopeptides; D009005:Monosaccharides; D037121:Plant Lectins; C040286:Tn antigen; C042242:Vicia lectins