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vwf, flow, gpibα, fig, pubmed, article, shear, binding, google, scholar, force, cas, willebrand, concatemers, factor, length, state, stress, domain, activation, tension, usa, dyn, rate, concatemer, fluor, nature, extension, relaxation, alexa, central, platelet, domains, cdot, nacl, monomer, supplementary, tensile, wall, data, number, free, intensity, fluorescence, kinetics, molecules, tethered, total, single, estimated,

Topics {✒️}

nature portfolio ez-link sulfo-nhs-lc-biotin privacy policy advertising open-book view thrombosis research custom-written matlab scripts protein-free media reprints profit research }}\hskip25pc\\ \frac{{{k_{{\rm{ donkey anti-rabbit igg development a1–gpibα receptor–ligand bond7 nature nature nature 466 von willebrand disease prevent multi-site attachment facilitate multi-point attachment research sulfosuccinimidyl-6-[biotin-amido] hexanoate low-affinity square shape high-affinity round shape c-terminal his6 tag von willebrand factor social media ni-nta affinity chromatography original author ph-regulated dimeric bouquet platelet glycoprotein ib-ix }}}} = \frac{{{k_{{\rm{ {1 - {\rm{exp}}\left supplementary movie 1 supplementary movie 2 supplementary movie 3 single-exponential decay dynamics water-glycerol mixture observed high-affinity sites develop von willebrand disease5 sepharose cl-2b access holes permissions long-range disulfide bond5 ultralarge vascular protein tension-dependent local transition tension-regulated conformational change protein-protein association kinetics cdot {k_{{\rm{ a1-domain flanking peptide

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         description:Von Willebrand factor, an ultralarge concatemeric blood protein, must bind to platelet GPIbα during bleeding to mediate hemostasis, but not in the normal circulation to avoid thrombosis. Von Willebrand factor is proposed to be mechanically activated by flow, but the mechanism remains unclear. Using microfluidics with single-molecule imaging, we simultaneously monitored reversible Von Willebrand factor extension and binding to GPIbα under flow. We show that Von Willebrand factor is activated through a two-step conformational transition: first, elongation from compact to linear form, and subsequently, a tension-dependent local transition to a state with high affinity for GPIbα. High-affinity sites develop only in upstream regions of VWF where tension exceeds ~21 pN and depend upon electrostatic interactions. Re-compaction of Von Willebrand factor is accelerated by intramolecular interactions and increases GPIbα dissociation rate. This mechanism enables VWF to be locally activated by hydrodynamic force in hemorrhage and rapidly deactivated downstream, providing a paradigm for hierarchical mechano-regulation of receptor–ligand binding. Von Willebrand factor (VWF) is a blood protein involved in clotting and is proposed to be activated by flow, but the mechanism is unknown. Here the authors show that VWF is first converted from a compact to linear form by flow, and is subsequently activated to bind GPIbα in a tension-dependent manner.
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      headline:Flow-induced elongation of von Willebrand factor precedes tension-dependent activation
      description:Von Willebrand factor, an ultralarge concatemeric blood protein, must bind to platelet GPIbα during bleeding to mediate hemostasis, but not in the normal circulation to avoid thrombosis. Von Willebrand factor is proposed to be mechanically activated by flow, but the mechanism remains unclear. Using microfluidics with single-molecule imaging, we simultaneously monitored reversible Von Willebrand factor extension and binding to GPIbα under flow. We show that Von Willebrand factor is activated through a two-step conformational transition: first, elongation from compact to linear form, and subsequently, a tension-dependent local transition to a state with high affinity for GPIbα. High-affinity sites develop only in upstream regions of VWF where tension exceeds ~21 pN and depend upon electrostatic interactions. Re-compaction of Von Willebrand factor is accelerated by intramolecular interactions and increases GPIbα dissociation rate. This mechanism enables VWF to be locally activated by hydrodynamic force in hemorrhage and rapidly deactivated downstream, providing a paradigm for hierarchical mechano-regulation of receptor–ligand binding. Von Willebrand factor (VWF) is a blood protein involved in clotting and is proposed to be activated by flow, but the mechanism is unknown. Here the authors show that VWF is first converted from a compact to linear form by flow, and is subsequently activated to bind GPIbα in a tension-dependent manner.
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