Coding

Part:BBa_K5374025:Design

Designed by: Yiqi Meng   Group: iGEM24_TestDaily-I-Beijing   (2024-09-24)


DDR.A receptor domain activated by collagen, playing a role in ECM remodeling.


Assembly Compatibility:
  • 10
    INCOMPATIBLE WITH RFC[10]
    Illegal EcoRI site found at 253
    Illegal EcoRI site found at 337
    Illegal EcoRI site found at 820
    Illegal PstI site found at 259
  • 12
    INCOMPATIBLE WITH RFC[12]
    Illegal EcoRI site found at 253
    Illegal EcoRI site found at 337
    Illegal EcoRI site found at 820
    Illegal PstI site found at 259
  • 21
    INCOMPATIBLE WITH RFC[21]
    Illegal EcoRI site found at 253
    Illegal EcoRI site found at 337
    Illegal EcoRI site found at 820
    Illegal BglII site found at 459
  • 23
    INCOMPATIBLE WITH RFC[23]
    Illegal EcoRI site found at 253
    Illegal EcoRI site found at 337
    Illegal EcoRI site found at 820
    Illegal PstI site found at 259
  • 25
    INCOMPATIBLE WITH RFC[25]
    Illegal EcoRI site found at 253
    Illegal EcoRI site found at 337
    Illegal EcoRI site found at 820
    Illegal PstI site found at 259
    Illegal NgoMIV site found at 588
  • 1000
    COMPATIBLE WITH RFC[1000]


Design Notes

The fusion protein was designed to balance the strong collagen-binding affinity of the FTD with the bioactivity of BMP-4. Codon optimization was applied to enhance expression in E. coli, ensuring efficient production and folding of the fusion protein. Special attention was given to preserving the osteogenic properties of BMP-4, allowing for controlled release and effective stimulation of bone formation when embedded in collagen matrices.


Source

The FTD is derived from proteins involved in ECM interactions, particularly those associated with collagen and tissue repair. BMP-4 is a well-characterized growth factor in the TGF-β superfamily that plays a crucial role in osteogenesis and bone healing.