Flaw-tolerance in silk fibrils explains strength, extensibility and toughness of spider silk

Silk is an ancient but remarkably strong, extensible and tough material made from simple protein building blocks. Earlier work has shown that the particular molecular geometry of silk with a composite of semi-amorphous and nanocrystalline beta-sheet protein domains provides the structural basis for its characteristic softening-stiffening behavior and remarkable strength at the nanoscale. Yet, an open question remains as to how these nanoscale properties are upscaled so effectively to create strong, extensible and tough silk fibers. Here we discover that the geometric confinement of fibrils to ≈50-100 nm width and arranged in bundles to form larger-scale silk fibers, is the key to explaining the upscaling of the mechanical properties of silk from the atomistic scale upwards. We find that under this geometric confinement, hundreds of thousands of protein domains unfold simultaneously and thereby act synergistically to resist deformation and failure, providing access to enhanced large-scale strength, extensibility and toughness. Moreover, since the material is in a flaw-tolerant state under this geometric confinement, structural inhomogeneities such as cavities or tears that typically act as stress concentrators do not compromise the material performance. Indeed, experimental work showed that the diameter of silk fibrils that make up larger-scale silk fibers are on the order of 20-100 nm, in agreement with our findings. The exploitation of this mechanism in engineering design enables the synthesis of hierarchical fiber materials for superior performance despite limited and inferior building blocks.