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Biomolecular recognition of glycosylated β 3 ‐peptides by GalNAc specific lectins
Author(s) -
Norgren Anna S.,
Geitmann Matthis,
Danielson U. Helena,
Arvidsson Per I.
Publication year - 2007
Publication title -
journal of molecular recognition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.401
H-Index - 79
eISSN - 1099-1352
pISSN - 0952-3499
DOI - 10.1002/jmr.821
Subject(s) - peptide , chemistry , biochemistry , glycosyl , residue (chemistry) , molecular recognition , galactose , glycosylation , peptide sequence , monomer , amino acid , stereochemistry , molecule , organic chemistry , gene , polymer
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 β 3 ‐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 β 3 ‐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.