Poster
30

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

Authors

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

Abstract

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.

Hosted By

ELRIG
The European Laboratory Research & Innovation Group Our Vision : To provide outstanding, leading edge knowledge to the life sciences community on an open access basis
Event Logo Find us on Facebook Follow us on Twitter

Get the App

Get this event information on your mobile by
going to the appstore or google play and search for 'elrig'
Login
Eventflo Home
copyright ELRIG, eventflo.co.uk, Labhoo Ltd 2003-2021