Diversity of C-linked neoglycopeptides for the exploration of subsite-assisted carbohydrate binding interactions.
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).
Arya
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P
Steacie Institute for Molecular Sciences, National Research Council of Canada, Ottawa, Ontario. Prabhat.Arya@nrc.ca
Kutterer
K M
KM
Qin
H
H
Roby
J
J
Barnes
M L
ML
Kim
J M
JM
Roy
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R
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
D004151:Dipeptides; D006020:Glycopeptides; D007202:Indicators and Reagents; D037102:Lectins; D037121:Plant Lectins; C034551:maclurin; D008239:Lysine