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

The staining results of a dish of CsgA-Mfp3S-pep bacteria with IPTG (Left) and a blank control dish of amilCP bacteria (Right)

After 9 days of SBF culture, THE MFP-CSGA was scanned by electron microscopy (compared with the sample on day 0).

SEM image showing the surface morphology of the biofilm (i.e., unmineralized). Scale bars:3μm

SEM image showing the surface morphology of the mineralized composite (mineralization 7d). Scale bars: 3μm

CsgA-Mfp3S-pep bacteria (Left) and amilCP bacteria (Right) cultured in SBF

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]