Part:BBa_K5298001
The 2xKLV-Mfp5 sequence can encode ordered amyloid proteins and disordered Mfp5 proteins, combining
This part selects the zipper-forming sequence from human Aβ amyloid protein due to its strong tendency to self-assemble into stable β-crystals under aqueous conditions. Then, a flexible sequence from the Nephila clavipes dragline spider silk protein MaSp1 is chosen to link multiple zipper-forming sequences together, allowing multiple zipper-forming sequences within a single protein to fold into β-sheets. The amyloid and spider silk sequences are repeated twice to achieve sufficient chain length, which is crucial for favorable material strength. To impart surface adhesion to the protein material, Mytilus galloprovincialis 5 (Mfp5) is then added to the C-terminus of the repeated sequences. In addition to surface adhesion, the disordered Mfp5 chains can also utilize dihydroxyphenylalanine (DOPA) and other amino acid residues to induce intermolecular interactions between hybrid proteins, thereby enhancing the cohesion of the material. Overall, the combination of ordered (amyloid) and disordered (Mfp5) sequences is expected to form β-crystals and amorphous domains, respectively, and the extensive intermolecular interaction network between the silk-amyloid-Mfp5 molecules (termed 2xKLV-Mfp5) can produce strong and tough semi-crystalline protein hydrogels that also exhibit underwater adhesion through surface-exposed DOPA residues in Mfp5.
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12INCOMPATIBLE WITH RFC[12]Illegal NotI site found at 5
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25INCOMPATIBLE WITH RFC[25]Illegal NgoMIV site found at 67
- 1000COMPATIBLE WITH RFC[1000]
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