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Studies on the interactions between glycosylated beta(3)-peptides and the lectin Vicia villosa by saturation transfer difference NMR spectroscopy
Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Biochemistry and Organic Chemistry.
Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Biochemistry and Organic Chemistry.
2009 (English)In: Carbohydrate Research, ISSN 0008-6215, E-ISSN 1873-426X, Vol. 344, no 18, 2577-2580 p.Article in journal (Refereed) Published
Abstract [en]

Saturation transfer difference (STD) NMR spectroscopy was used to study the interaction of the lectin Vicia villosa (VVLB4) 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.

Place, publisher, year, edition, pages
2009. Vol. 344, no 18, 2577-2580 p.
Keyword [en]
STD NMR, Glycosylated beta(3)-peptides, Tn antigen, Lectin Vicia villosa (isolectin B-4)
National Category
Biochemistry and Molecular Biology
Identifiers
URN: urn:nbn:se:uu:diva-148210DOI: 10.1016/j.carres.2009.06.040ISI: 000272860500022PubMedID: 19863951OAI: oai:DiVA.org:uu-148210DiVA: diva2:401645
Available from: 2011-03-03 Created: 2011-03-03 Last updated: 2017-12-11Bibliographically approved

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