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Microfluidic Dry-spinning and Characterization of Regenerated Silk Fibroin Fibers
Published on: September 4, 2017
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Spider silk self-assembly via modular liquid-liquid phase separation and nanofibrillation
Ali D Malay1, Takehiro Suzuki2, Takuya Katashima3
1Biomacromolecules Research Team, RIKEN Center for Sustainable Resource Science, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan. a.malay@riken.jp keiji.numata@riken.jp.
Science Advances
|November 5, 2020
Summary
Spider silk rapidly self-assembles via liquid-liquid phase separation (LLPS) triggered by anions and acidification. This process, involving spidroin protein domains, forms hierarchical fibers, offering insights into biomaterial formation.
Area of Science:
- Biochemistry
- Materials Science
- Biomimetics
Background:
- Spider silk fiber formation from spidroin protein is not fully understood.
- The process involves soluble spidroin protein transitioning to insoluble fiber.
Purpose of the Study:
- To present an integrated model for spider silk formation.
- To elucidate the roles of chemical and physical gradients on spidroin domains during assembly.
Main Methods:
- Developing a model incorporating chemical and physical gradients.
- Investigating the role of liquid-liquid phase separation (LLPS) mediated by spidroin domains.
- Analyzing the effects of acidification and mechanical stress on silk assembly.
Main Results:
- LLPS is triggered by multivalent anions (e.g., phosphate) and mediated by carboxyl-terminal and repetitive domains.
- Acidification and LLPS initiate nanofibril network self-assembly, facilitated by amino-terminal domain dimerization.
- Liquid-to-solid phase transition occurs, and mechanical stress leads to hierarchical fibers with beta-sheet structures.
- Findings were corroborated using native silk gland material.
Conclusions:
- The study presents a comprehensive model for spider silk formation.
- Silk assembly shares parallels with intracellular membraneless organelles and protein aggregation disorders.
- The findings advance understanding of natural biomaterial fabrication and LLPS mechanisms.
