Kraig Biocraft Laboratories Inc (KBLB)

[TRUISM]

We demonstrate that fibers of a ~60kDa bi-terminally fused amyloid-silk protein exhibit ultimate tensile strength up to 481±31MPa and toughness of 179±39 MJ*m-3, while achieving a high titer of 8.0±?0.70g/L by bioreactor production.

We show that bi-terminal fusion of Mfp5 fragments significantly enhances the alignment of ß-nanocrystals, and intermolecular interactions are promoted by cation-p and p-p interactions between terminal fragments. Our approach highlights the advantage of self-interacting intrinsically-disordered proteins in enhancing material mechanical properties and can be applied to a wide range of protein-based materials.

Bi-terminal fusion of intrinsically-disordered mussel foot protein fragments boosts mechanical strength for protein fibers












TRUISM