Authors:Keiji Numata1, Ryota Sato1,2, Kenjiro Yazawa1, Takaaki Hikima3, Hiroyasu Masunaga4
DOI: 10.1016/j.polymer.2015.09.025
- 1. Enzyme Research Team, Biomass Engineering Program Cooperative Division, RIKEN Center for Sustainable Resource Science
- 2. Spiber Inc.
- 3. RIKEN SPring-8 Center
- 4. Japan Synchrotron Radiation Research Institute
Abstract
Antheraea yamamai silk contains long poly(alanine) sequences that contribute to β-sheet crystals, which are responsible for the high tensile strength of silk fibers. We determined the crystal structure, physical properties, and morphology of A. yamamai cocoon silk fibers. The crystal lattice of A. yamamai silk fiber consists of antiparallel β-pleated sheets with an orthogonal unit cell (a = 10.72 Å, b = 9.73 Å, c [fiber axis] = 6.80 ± 0.05 Å). Wide-angle X-ray scattering and birefringence measurements revealed that stretching deformation does not affect the crystal structure but contributes to alignment of silk molecules along the fiber axis in the partial amorphous phase. Crystallinity and amino acid sequence analyses suggested that the poly(alanine) region can be partially crystallized. The long poly(alanine) sequences therefore do not contribute to the mechanical, thermal, or structural properties of A. yamamai silk. Our results may aid the design and development of A. yamamai silk-based materials.
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本研究の遂行に際し、当社は 内閣府 革新的研究開発推進プログラム(ImPACT)「超高機能構造タンパク質による素材産業革命」の助成を受けました。