Biomolecular Recognition of Glycosylated β3-Peptides by GalNAc Specific Lectins
2007 (English)In: Journal of Molecular Recognition, ISSN 0952-3499, E-ISSN 1099-1352, Vol. 20, no 2, 132-138 p.Article in journal (Refereed) Published
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.
Place, publisher, year, edition, pages
2007. Vol. 20, no 2, 132-138 p.
b-peptides, glycopeptides, lectins, molecular recognition, surface plasmon resonance
IdentifiersURN: urn:nbn:se:uu:diva-95281DOI: 10.1002/jmr.821ISI: 000246169000008PubMedID: 17410519OAI: oai:DiVA.org:uu-95281DiVA: diva2:169440