Unveiling the secrets of the mechanism of spider silk assembly

August 28, 2024

How does the self-assembly of spider silk proteins with different hydrophobicities progress?

The collaborative research team from the RIKEN CSRS and Kyoto University has elucidated the process by which spider silk is assembled into insoluble fiber with a complex hierarchical structure. This achievement is expected to contribute to the development of next-generation fiber materials that are both highly efficient and environmentally friendly.

The collaborative research team developed a new platform for producing MaSp1, the main protein component of spider dragline silk. By using the platform, they revealed the factors that enable MaSp1 to assemble from disordered proteins into more complex structures gradually, and then mimicked the silk assembly process inside spiders successfully. This process occurs along with liquid-liquid phase separation (LLPS) in response to ion gradients, nanofiber formation in response to pH gradients, and the induction of β-sheet structures in response to mechanical deformation. These changes synergistically induce the self-assembly of nanofibers with an oriented internal structure. Notably, the self-assembly of MaSp1 with great rapidity was observed using newly developed monitoring techniques.

Original article

Advanced Functional Materials doi: 10.1002/adfm.202408175

A. D. Malay, N. A. Oktaviani, J. Chen, K. Numata,

"Spider silk: Rapid, bottom-up self-assembly of MaSp1 into hierarchically structured fibers through biomimetic processing".

Contact

Keiji Numata; Team Leader
Ali D. Malay; Senior Scientist
Biomacromolecules Research Team