Assessing the inhibitory potency of galectin ligands identified from combinatorial (glyco)peptide libraries using surface plasmon resonance spectroscopy

C.E.P. Maljaars, S. André, K.M. Halkes, H.-J. Gabius, J.P. Kamerling

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Combinatorial (glyco)peptide libraries offer the possibility to define effective inhibitors of protein (lectin)– glycan interactions. If a (glyco)peptide surpasses the inhibitory potency of the free sugar, then the new peptide–lectin contacts underlying the affinity enhancement may guide further rational drug design. Focusing on the adhesion/growth regulatory human galectins 1 and 3, a screening of three combinatorial solid-phase (glyco)peptide libraries, containing Gal(b1-O)Thr, Gal(b1-S)Cys/Gal(b1-N)Asn, and Lac(b1- O)Thr, with the fluorescently labeled lectins had led to a series of lead compounds. To define the inhibitory potency of a selection of resynthesized (glyco)peptides systematically, a surface plasmon resonance-based inhibition assay with immobilized asialofetuin was set up. (Glyco)Peptides with up to 66-fold potency relative to free lactose as inhibitor were characterized. The presence of lactose in the most effective glycopeptides indicated the presence of affinity-enhancing peptide–lectin contacts. In addition to drug design, they may be helpful for fine-structural analysis of the binding sites.
Original languageUndefined/Unknown
Pages (from-to)190-196
Number of pages7
JournalAnalytical Biochemistry
Issue number2
Publication statusPublished - 2008

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