title: Biomolecular recognition of glycosylated beta(3)-peptides by GalNAc specific lectins.
abstract: The molecular recognition of a novel kind of hybrid conjugates, composed of artificial biomimetic beta-peptide oligomers with an O-linked natural N-acetyl-galactosamine (the Tn-antigen) residue, by four different GalNAc specific lectins was investigated using surface plasmon biosensor technology. The influence of the peptide and the glycosyl moiety on the recognition was studied using two glycosylated beta(3)-heptapeptides, a glycosylated alpha-heptapeptide, two beta-amino acid containing dipeptides, and monomeric alphaGalNAc-O-Thr. Although all four lectins displayed a decreased affinity for the carbohydrate residue when attached to a peptide, as compared to the monomeric Tn-antigen, the peptide part was found to have distinct effects on the binding kinetics-indicating that varying degrees of protein-peptide interactions occurred in the recognition process. Likewise, the lectins did not discriminate between beta(3)-peptides and the alpha-peptide, but the beta-linkage of the galactose had a detrimental effect for at least two of the lectins.
authors.affiliation: Department of Biochemistry and Organic Chemistry, Uppsala University, Sweden.
authors.forename: Anna S
authors.initials: AS
authors.lastname: Norgren
authors.forename: Matthis
authors.initials: M
authors.lastname: Geitmann
authors.forename: U Helena
authors.initials: UH
authors.lastname: Danielson
authors.forename: Per I
authors.initials: PI
authors.lastname: Arvidsson
mesh_terms: D000116:Acetylgalactosamine / Q000737:chemistry* / Q000378:metabolism; D002240:Carbohydrate Sequence; D006020:Glycopeptides / Q000737:chemistry* / Q000378:metabolism*; D007700:Kinetics; D037102:Lectins / Q000737:chemistry* / Q000378:metabolism*; D008954:Models, Biological; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011485:Protein Binding
chemical_list: D006020:Glycopeptides; D037102:Lectins; D000116:Acetylgalactosamine