Studies on the interactions between glycosylated beta3-peptides and the lectin Vicia villosa by saturation transfer difference NMR spectroscopy

Marta Kaszowska; Anna S Norgren; Per I Arvidson; Corine Sandström

doi:10.1016/j.carres.2009.06.040

Studies on the interactions between glycosylated beta3-peptides and the lectin Vicia villosa by saturation transfer difference NMR spectroscopy

Carbohydr Res. 2009 Dec 14;344(18):2577-80. doi: 10.1016/j.carres.2009.06.040. Epub 2009 Jul 4.

Authors

Marta Kaszowska¹, Anna S Norgren, Per I Arvidson, Corine Sandström

Affiliation

¹ Department of Chemistry, Swedish University of Agricultural Sciences, PO Box 7015, SE-750 07 Uppsala, Sweden.

PMID: 19863951
DOI: 10.1016/j.carres.2009.06.040

Abstract

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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Antigens, Tumor-Associated, Carbohydrate
Glycopeptides / chemistry*
Magnetic Resonance Spectroscopy / methods*
Molecular Conformation
Monosaccharides
Plant Lectins / chemistry*
Protein Binding

Substances

Antigens, Tumor-Associated, Carbohydrate
Glycopeptides
Monosaccharides
Plant Lectins
Tn antigen
Vicia lectins