Fig. 5: Biophysical characterization of A107 and the inhibitory mechanism studies. | Nature Communications

Fig. 5: Biophysical characterization of A107 and the inhibitory mechanism studies.

From: Harnessing indole scaffolds to identify small-molecule IRE1α inhibitors modulating XBP1 mRNA splicing

Fig. 5

a Michaelis–Menten kinetic study revealed IA107 as a noncompetitive inhibitor of the XBP1 mRNA. n = 2. b Competition experiments in ITC by titrating 200 μM G1749 to 10 μM IRE1α pre-incubated with DMSO and different concentrations of IA107 (50 μM, 200 μM, 1 mM), respectively. c KD of the competition experiments in ITC by the titration of 200 μM G1749 to IRE1α pre-incubated with different concentrations of IA107, IA34, or DMSO. d Table of KD values obtained from competition ITC experiments by titrating IA107 to IRE1α pre-incubated with DMSO or different concentrations of G1749. ND, not detectable. e The kinase inhibitory activities of IA01, IA06, IA10, IA64, and IA107 against IRE1α in the LanthaScreenTM Eu kinase binding assay (Thermo Fisher SelectScreen), n = 2.

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