Biomolecular Recognition of Glycosylated Peptides by GalNAc Specific Lectins

01 January 2007

Norgren, A.S., Geitmann, M., Danielson, U.H., Arvidsson, P.I. (2007) J. Molecular Recognition 20: 132-138

The molecular recognition of a novel kind of hybrid conjugates, composed of artificial biomimetic β-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 β3-heptapeptides, a glycosylated α-heptapeptide, two β-amino acid containing dipeptides, and monomeric αGalNAc-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 β3-peptides and the α-peptide, but the β-linkage of the galactose had a detrimental effect for at least two of the lectins. Copyright © 2007 John Wiley & Sons, Ltd.

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