Animal hairs, like other natural fibers, display excellent mechanical properties, especially, the tensile toughness and fracture resistance. Several structure-mechanics models have attributed mechanical superiority of hair to its unique nanocomposite structure which consists of intermediate filaments and matrix. However, the contribution of fibrils and their associated interfaces on the mechanical properties of animal hairs remains unclear. Herein, using the small- and wide-angle X-ray scattering, and an ultrahigh-speed microcamera system, it is confirmed that the conformation and fibrils (which represent both nanofibrils and microfibrils) of the keratin channel endow tensile toughness and fracture resistance to camel hairs. During the stretching process, an α-β transition occurred at the secondary structure level, leading to the formation of a tensile plateau, which improves the toughness compared with the structure without a conformation transition. Meanwhile, fibrils further toughened the camel hairs and resisted their crack propagation through confined fibrillar slippage, splitting, and pulling. These structure-property relations in natural hairs can inspire damage-tolerant polymer fiber design.
Keywords: fibril; hair; mechanical property; secondary structure; structure−property relationship.