Difference between revisions of "Part:BBa K3672005"
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A collagen binding domain (CBD) WREPSFCALS, which was identified from von Willebrand Factor (vWF), exhibits low binding affinity (Kd: 100 μM) for collagen type I  
 
A collagen binding domain (CBD) WREPSFCALS, which was identified from von Willebrand Factor (vWF), exhibits low binding affinity (Kd: 100 μM) for collagen type I  
  
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===Usage and Biology===
 
===Usage and Biology===
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===This could be new information learned from literature===
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1. "Analysis of the role of von Willebrand factor, platelet glycoprotein VI-, and α2β1-mediated collagen binding in thrombus formation" (2014)
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====Research Background and Purpose====
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This study investigates the role of collagen-binding mutations in the A3 domain of von Willebrand Factor (VWF) in thrombus formation. VWF is a key protein in the coagulation process, binding to exposed subendothelial collagen to initiate platelet adhesion and thrombus formation. The main goal is to analyze these collagen-binding mutants' effects on VWF function through mouse models and in vitro experiments.
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Revision as of 14:57, 14 September 2024


Type4,CBD probe for collagen I

A collagen binding domain (CBD) WREPSFCALS, which was identified from von Willebrand Factor (vWF), exhibits low binding affinity (Kd: 100 μM) for collagen type I

Usage and Biology

This could be new information learned from literature

1. "Analysis of the role of von Willebrand factor, platelet glycoprotein VI-, and α2β1-mediated collagen binding in thrombus formation" (2014)

Research Background and Purpose

This study investigates the role of collagen-binding mutations in the A3 domain of von Willebrand Factor (VWF) in thrombus formation. VWF is a key protein in the coagulation process, binding to exposed subendothelial collagen to initiate platelet adhesion and thrombus formation. The main goal is to analyze these collagen-binding mutants' effects on VWF function through mouse models and in vitro experiments.


Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    COMPATIBLE WITH RFC[25]
  • 1000
    COMPATIBLE WITH RFC[1000]


References


  1. Wahyudi H, Reynolds AA, Li Y, Owen SC, Yu SM. Targeting collagen for diagnostic imaging and therapeutic delivery. J Control Release. 2016;240:323-331. doi:10.1016/j.jconrel.2016.01.007
  2. Takagi J, Asai H, Saito Y. A collagen/gelatin-binding decapeptide derived from bovine propolypeptide of von Willebrand factor. Biochemistry. 1992;31:8530–8534.
  3. Zhao W, Chen B, Li X, Lin H, Sun W, Zhao Y, Han Q, Dai J. Vascularization and cellularization of collagen scaffolds incorporated with two different collagen-targeting human basic fibroblast growth factors. J Biomed Mater Res. 2007;82A:630–636.