Part:BBa_K4055531
pT7-B0034-csgA_linker_mfp3spep
Biofilm structural proteins in E. coli fused with mussel foot protein(Mfp) analogs bestowed the engineered biofilms with HA mineralization-promoting and interfacial binding roles. When a blue light-induced strain was used to grow functional biofilms with controlled spatial and biomass density, living mineralized materials with patterning and gradient features could be generated following a benign biomimetic HA mineralization process.
an Mfp3S protein could initiate HA mineralization and promote interfacial adhesion.CsgA–Mfp fusion proteins comprising a CsgA domain (major protein component of the E. coli biofilm31) and a C-terminal Mfp serial fusion domain were constructed.
Moreover, examination of in vivo mineralization by TEM confirmed that CsgA–Mfp3S-pep-expressing biofilms triggered denser mineral formation with more apparent crystalline features after 5 d of min-eralization . These results thus highlight the roles of the Mfp3S-pep fusion protein in promoting HA mineral formation and crystallization.
Experiment
Staining results of protein expressed by plasmid PT7-B0034-CSGA_linker_mFP3SPEP
图0
After 9 days of SBF culture, THE MFP-CSGA was scanned by electron microscopy (compared with the sample on day 0).
图1
The surface morphology of biofilms was 5μm by scanning electron microscopy
图2
The surface morphology of biofilms was 5μm by scanning electron microscopy
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]
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