FigureĀ 3.
BT200 concentration-dependently inhibits VWF interaction with LRP1 cluster II and cluster IV. (A-D) BT200 significantly inhibits binding of human pdVWF (A); commercial rVWF (B); VWF-A1A2A3 truncation (C); and isolated VWF-A1 domain (D) to purified LRP1 cluster II (blue) and cluster IV (red) in a concentration-dependent manner. (E-F) BT100 (blue) and BT200 (red) significantly inhibit the binding of VWF-A1A2A3 to LRP1 cluster II (E) and LRP1 cluster IV (F). Plate binding (%) is calculated from absorbance at 450 nm in which the value for 0-nM BT200 or BT100 was taken as 100%. Dots represent the mean plate binding (%) at corresponding aptamer concentrations. Error bars depict the standard deviations. P values are outcomes of extra-sum-of-squares F test and compare the binding capacity of pdVWF vs rVWF or VWF constructs with LRP1 cluster II and cluster IV. Abs, absorbance; pdVWF, plasma-derived VWF; rVWF, recombinant VWF.

BT200 concentration-dependently inhibits VWF interaction with LRP1 cluster II and cluster IV. (A-D) BT200 significantly inhibits binding of human pdVWF (A); commercial rVWF (B); VWF-A1A2A3 truncation (C); and isolated VWF-A1 domain (D) to purified LRP1 cluster II (blue) and cluster IV (red) in a concentration-dependent manner. (E-F) BT100 (blue) and BT200 (red) significantly inhibit the binding of VWF-A1A2A3 to LRP1 cluster II (E) and LRP1 cluster IV (F). Plate binding (%) is calculated from absorbance at 450 nm in which the value for 0-nM BT200 or BT100 was taken as 100%. Dots represent the mean plate binding (%) at corresponding aptamer concentrations. Error bars depict the standard deviations. P values are outcomes of extra-sum-of-squares F test and compare the binding capacity of pdVWF vs rVWF or VWF constructs with LRP1 cluster II and cluster IV. Abs, absorbance; pdVWF, plasma-derived VWF; rVWF, recombinant VWF.

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