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. Author manuscript; available in PMC: 2020 Feb 14.
Published in final edited form as: J Med Chem. 2018 Dec 5;62(3):1125–1137. doi: 10.1021/acs.jmedchem.8b00513

Figure 2. Identification of 1 as a novel inhibitor of SHP2.

Figure 2.

Figure 2.

(A) Chemical structure of 1. (B) Phosphatase assays were carried out using full length SHP2 or SHP1 as the enzyme and a phospho-peptide as the substrate in the presence of various concentrations of 1, as described in Experimental Section. For IC50 determinations, six concentrations of 1 were tested. Results shown are the mean ± SD of three independent experiments. (C) Phosphatase activities of full length WT SHP2, full length SHP2 E76K, and the SHP2 PTP domain were assessed in the presence of 1 at various concentrations as above. IC50 values were then determined. Experiments were repeated independently three times, similar results were obtained in each experiment. Results shown are the mean ± SD of triplicates from one experiment. (D) Phosphatase activities of full length WT SHP2, full length SHP2 E76K, and the SHP2 PTP domain were determined in the presence of 1 (10 μM) using a phospho-peptide or pNPP as the substrate, as detailed in Experimental Section Experiments were repeated independently three times, similar results were obtained in each experiment. Results shown are the mean ± SD of triplicates from one experiment.