A Mini-Spidroin Forms High-Performance Artificial Spider Silk via Edge-Cysteine-Locked β-Sheet Assembly.

ABSTRACT: Spider silk's remarkable mechanical properties arise from its hierarchical organization, where β-sheet nanocrystals confer strength and amorphous chains impart extensibility. However, replicating this performance in synthetic fibers has been hindered by the challenges of expressing high-molecular-weight spidroins and processing them into fibers. Here, we overcome these limitations by engineering a mini-spidroin (∼33 kDa) that is both easily expressible and spinnable, yet yields fibers with exceptional strength and toughness. Our strategy introduces cysteine residues at the termini of polyalanine (polyA) segments, enabling inter-strand disulfide bonds that enhance molecular cohesion during liquid-liquid phase separation (LLPS). This "edge-cysteine locking" promotes directional β-sheet assem

SUBMITTER: Li M 

PROVIDER: S-EPMC12915095 | biostudies-literature | 2026 Feb

REPOSITORIES: biostudies-literature