The development and characterization of a long acting anti-thrombotic von Willebrand factor (VWF) aptamer.

A P < .05 was considered significant and a Bonferroni correction applies to multiple comparisons (eg, tirofiban and BT200 vs control), but P ‐value corrections were not performed for post‐hoc tests in which the ANOVA was highly significant and concentration‐ and/or time‐dependent effects were tested. 3 RESULTS 3.1 Cocrystallization of BT100 with vWF A1 domain Multiple nucleotides of BT‐100 directly interacted with amino acid residues of the recombinant VWF A1 domain, and mostly these nucleotides reside in the loop, suggesting that the loop sequences provided the VWF A1 domain binding interaction while the stem sequences provided the aptamer structural stability.

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