Diversity of C-linked neoglycopeptides for the exploration of subsite-assisted carbohydrate binding interactions

Diversity of α-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 α-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). Diversity of α-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 α-galactoside units on the side chain of the lysine residue of the dipeptide backbone, exhibited a most remarkable effect with a 2.82 fold increase in its inhibitory properties (IC50 1.48 mM) in comparison to 1b (IC50 4.18 mM).