title: Diversity of C-linked neoglycopeptides for the exploration of subsite-assisted carbohydrate binding interactions.
abstract: Diversity of alpha-galactose based C-linked neoglycopeptides (1b, 2b, 3c, 4d, and 5d) has been developed to explore the importance of subsite-assisted carbohydrate binding interactions. Deprotected C-linked neoglycopeptides (1b, 2b, 3c, 4d, and 5d) were synthesized and tested in competitive inhibition assays using a model enzyme-linked lectin (e.g., Maclura pomifera). Compound 2b, with two alpha-galactoside units on the side chain of the lysine residue of the dipeptide backbone, exhibited a remarkable effect with a 2.82-fold increase in its inhibitory properties (IC50 1.48 mM) in comparison to 1b (IC50 4.18 mM).
authors.affiliation: Steacie Institute for Molecular Sciences, National Research Council of Canada, Ottawa, Ontario. Prabhat.Arya@nrc.ca
authors.forename: P
authors.initials: P
authors.lastname: Arya
authors.forename: K M
authors.initials: KM
authors.lastname: Kutterer
authors.forename: H
authors.initials: H
authors.lastname: Qin
authors.forename: J
authors.initials: J
authors.lastname: Roby
authors.forename: M L
authors.initials: ML
authors.lastname: Barnes
authors.forename: J M
authors.initials: JM
authors.lastname: Kim
authors.forename: R
authors.initials: R
authors.lastname: Roy
mesh_terms: D001665:Binding Sites; D001667:Binding, Competitive; D004151:Dipeptides / Q000138:chemical synthesis / Q000737:chemistry / Q000494:pharmacology; D006020:Glycopeptides / Q000138:chemical synthesis* / Q000737:chemistry / Q000378:metabolism; D007202:Indicators and Reagents; D037102:Lectins / Q000737:chemistry; D008239:Lysine; D008958:Models, Molecular; D037121:Plant Lectins; D013329:Structure-Activity Relationship
chemical_list: D004151:Dipeptides; D006020:Glycopeptides; D007202:Indicators and Reagents; D037102:Lectins; D037121:Plant Lectins; C034551:maclurin; D008239:Lysine