Fig. 5: VHH81 binds to the NAIM to inhibit the A1-GPIbα interaction. | Nature Communications

Fig. 5: VHH81 binds to the NAIM to inhibit the A1-GPIbα interaction.

From: Activation of von Willebrand factor via mechanical unfolding of its discontinuous autoinhibitory module

Fig. 5

Sensorgrams of immobilized AIM-A1 (A) or A1-CAIM (B) binding to serial dilutions of VHH81 from 1 μM to 15.6 nM. Global curve fits are displayed in red over binding traces. Fitted equilibrium dissociation constants are shown as globally fitted value ± standard deviation of the fit. No observable binding response was detected for A1-CAIM. C Steady-state binding curves of VWF constructs to VHH81. Binding data are shown in (A, B) and Supplementary Fig. 14 are plotted and fit to a hyperbola. tAIM-A1 comprises residues 1261–1472. Washed platelet aggregation responses to AIM-A1 (D) and A1-CAIM (E) pre-incubated with 0, 1, or 2 μM VHH81. F Comparison of relative inhibition of washed platelet aggregation using various concentrations of VHH81. In all cases, 1 μM VWF fragments were used. Data are means ± standard deviation, n = 3 per condition. Source data are provided in a worksheet of the Source Data file.

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