Part:BBa_K3672005

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

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.