Wijeratne, Sithara S.Li, JingqiangYeh, Hui-ChunNolasco, LeticiaZhou, ZhouBergeron, AngelaFrey, Eric W.Moake, Joel L.Dong, Jing-feiKiang, Ching-Hwa2016-05-022016-05-022016Wijeratne, Sithara S., Li, Jingqiang, Yeh, Hui-Chun, et al.. "Single-molecule force measurements of the polymerizing dimeric subunit of von Willebrand factor." <i>Physical Review E,</i> 93, no. 1 (2016) American Physical Society: 012410. http://dx.doi.org/10.1103/PhysRevE.93.012410.https://hdl.handle.net/1911/90387Von Willebrand factor (VWF) multimers are large adhesive proteins that are essential to the initiation of hemostatic plugs at sites of vascular injury. The binding of VWF multimers to platelets, as well as VWF proteolysis, is regulated by shear stresses that alter VWF multimeric conformation. We used single molecule manipulation with atomic force microscopy (AFM) to investigate the effect of high fluid shear stress on soluble dimeric and multimeric forms of VWF. VWF dimers are the smallest unit that polymerizes to construct large VWF multimers. The resistance to mechanical unfolding with or without exposure to shear stress was used to evaluate VWF conformational forms. Our data indicate that, unlike recombinant VWF multimers (RVWF), recombinant dimeric VWF (RDVWF) unfolding force is not altered by high shear stress (100dynes/cm2 for 3 min at 37∘C). We conclude that under the shear conditions used (100dynes/cm2 for 3 min at 37∘C), VWF dimers do not self-associate into a conformation analogous to that attained by sheared large VWF multimers.engArticle is made available in accordance with the publisher's policy and may be subject to US copyright law. Please refer to the publisher's site for terms of use.Journal articlehttp://dx.doi.org/10.1103/PhysRevE.93.012410