Biomolecular recognition of glycosylated beta(3)-peptides by GalNAc specific lectins.
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.
Norgren
Anna S
AS
Department of Biochemistry and Organic Chemistry, Uppsala University, Sweden.
Geitmann
Matthis
M
Danielson
U Helena
UH
Arvidsson
Per I
PI
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
D006020:Glycopeptides; D037102:Lectins; D000116:Acetylgalactosamine