Determination of the affinity and kinetic rate constants of galectin inhibitors using surface plasmon resonance.


J Mabbitt1; J Roper1; R Slack1
1 Galecto, Inc., UK


The galectins are a family of 15 soluble cytosolic proteins found in mammals that are defined by structurally similar carbohydrate recognition domains (CRD) that recognize sugar residues on the surface of cells. They can form lattices that control glycoprotein localization, protein trafficking & receptor/enzyme concentration or availability & have been implicated in several cellular processes. Certain galectins have also been shown to be implicated in fibrotic and cancer indications with therapeutics now being investigated in early clinical studies. For the development of small molecule inhibitors of galectins, historically the standard approaches for determining affinity and selectivity have been fluorescence polarization or homogenous time-resolved fluorescence. In this study we investigated surface plasmon resonance (SPR) as an alternative approach for defining mouse/human galectin-1 & galectin-3 affinity & selectivity with the additional focus on association & dissociation kinetics for these interactions.

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