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Mechanical activation of a multimeric adhesive protein through domain conformational change
- Source :
- Physical review letters. 110(10)
- Publication Year :
- 2012
-
Abstract
- The mechanical force-induced activation of the adhesive protein von Willebrand Factor (VWF), which experiences high hydrodynamic forces, is essential in initiating platelet adhesion. The importance of the mechanical force-induced functional change is manifested in the multimeric VWF’s crucial role in blood coagulation, when high fluid shear stress activates plasma VWF (pVWF) multimers to bind platelets. Here we showed that a pathological level of high shear stress exposure of pVWF multimers results in domain conformational changes, and the subsequent shifts in the unfolding force allow us to use force as a marker to track the dynamic states of multimeric VWF. We found that shear-activated pVWF multimers (spVWF) are more resistant to mechanical unfolding than non-sheared pVWF multimers, as indicated in the higher peak unfolding force. These results provide insight into the mechanism of shear-induced activation of pVWF multimers.
- Subjects :
- Conformational change
biology
Platelet Aggregation
Chemistry
Protein Conformation
General Physics and Astronomy
Fluid shear stress
Nanotechnology
Models, Biological
Article
Protein Structure, Tertiary
Protein structure
Von Willebrand factor
Coagulation
hemic and lymphatic diseases
von Willebrand Factor
biology.protein
Unfolded protein response
Biophysics
Thermodynamics
Platelet
Adhesive
Protein Unfolding
Subjects
Details
- ISSN :
- 10797114
- Volume :
- 110
- Issue :
- 10
- Database :
- OpenAIRE
- Journal :
- Physical review letters
- Accession number :
- edsair.doi.dedup.....95452a4afafa69716e600a462fe1c681