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. 2012 Nov 6;287(53):44694–44702. doi: 10.1074/jbc.M111.309450

FIGURE 3.

FIGURE 3.

Both BTT-3033 and BTT-3034 bind to the α2I domain but only the function of BTT-3033 is dependent on Tyr-285. A, the adhesion of CHO-α2Y285F cells to collagen I in the presence or absence of the integrin inhibitors BTT-3033, BTT-3034, or BTT-3016 (at EC50 concentrations) was evaluated. Adherent cells were detected using the WST-1 reagent. BTT-3034, unlike BTT-3033 or BTT-3016, inhibited the adhesion of CHO-α2Y285F cells to collagen I, indicating that BTT-3033 and BTT-3016 bind to the α2I MIDAS motif. The data expressed are the mean ± S.E. of three independent experiments. Significant difference between BTT-3033 and BTT-3034 is indicated by an asterisk (Student's t test, *, p = 0.05). B, the thermal stability of wt and E318W recombinant α2I domains in the presence or absence of BTT-3033 (42 μm) or BTT-3034 (49 μm) and 1 mm Mg2+ was studied using differential scanning fluorimetry. Both BTT-3033 and BTT-3034 decreased the thermal stability of the α2I wt domain in the presence of Mg2+.