Abstract
Various natural protein materials have hierarchical microscale and nanoscale structures that protect animals from suffering cold weather or external threats. Herein, we contribute an effective strategy for exploring the hierarchical structure transformation mechanism by stretching a single fiber and bundle fibers. Taking advantage of controllable stretching, the disulfide bonds and peptide chains were taken apart or reconstructed by the new crosslinking bonds inside the wool fiber. If the temperature, solution concentration and stretching velocity were appropriate, the strain was more than 230% and the microstructure transformation of a single fiber underwent α→ β transition, disulfide bond breakage and macromolecule slippage occurred during the tensile process. The transformation mechanism was modeled and experimentally tested in wool bundle fibers after setting, suggesting that the stretching led to the transformation from α helix to β-pleated sheet, the breakage of disulfide bonds and the slippage of microfibrils. The availability of wool fibers provides many opportunities for bio-friendly cellular substrates and biosensor devices.
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