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

ABSTRACT:

Background

Thrombus formation involves coagulation proteins and platelets. The latter, referred to as platelet-mediated thrombogenesis, is predominant in arterial circulation. Platelet thrombogenesis follows vascular injury when extracellular von Willebrand factor (VWF) binds via its A3 domain to exposed collagen, and the free VWF A1 domain binds to platelet glycoprotein Ib (GPIb).

Objectives

To characterize the antiplatelet/antithrombotic activity of the pegylated VWF antagonist aptamer BT200 and identify the aptamer VWF binding site.

Methods

BT100 is an optimized aptamer synthesized by solid-phase chemistry and pegylated (BT200) by standard conjugation chemistry. The affinity of BT200 for purified human VWF was evaluated as was VWF inhibition in monkey and human pla

SUBMITTER: Zhu S 

PROVIDER: S-EPMC7317574 | biostudies-literature | 2020 May

REPOSITORIES: biostudies-literature