The DOI matches its Crossref record; 25 of the 25 references it cites were found in a registry or an index.
Structural Origin of the Strain‐Hardening of Spider Silk
Abstract
Spider dragline silk, as a type of high‐performance natural fiber, displays a unique combination of tensile strength and extensibility that gives rise to a greater toughness than any other natural or synthetic fiber. In contrast to silkworm silk, spider dragline silk displays a remarkable strain‐hardening character for which the origin remains unknown. In this paper, the performance of silkworm silk and spider dragline fibers under stretching is compared based on a combined structural and mechanical analysis. The molecular origin of the strain‐hardening of spider silk filaments is addressed in comparison to rubber and Kevlar. Unlike rubber, the occurrence of strain‐hardening can be attributed to the unfolding of the intramolecular β‐sheets in spider silk fibrils, which serve as “molecular spindles” to store lengthy molecular chains in space compactly. With the progressive unfolding and alignment of protein during fiber extension, protein backbones and nodes of the molecular network are stretched to support the load. Consequently the dragline filaments become gradually hardened, enabling efficient energy buffering when an abseiling spider escapes from a predator. As distinct from synthetic materials such as rubber (elastomers), this particular structural feature of spider draglines not only enables quick energy absorption, but also efficiently suppresses the drastic oscillation which occurs upon an impact. The mimicking of this strain‐hardening character of spider silk will give rise to the design and fabrication of new advanced functional materials with applications in kinetic energy buffering and absorption.
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Cites
Reversible Unfolding of Individual Titin Immunoglobulin Domains by AFM
Rief, M., Gautel, M., Oesterhelt, F., Fernandez, J. M., & Gaub, H. E. (1997) · Science · doi:10.1126/science.276.5315.1109 · Cited by 3,077
Smith, S. B., Cui, Y., & Bustamante, C. (1996) · Science · doi:10.1126/science.271.5250.795 · Cited by 2,770
Liquid crystalline spinning of spider silk
Vollrath, F., & Knight, D. P. (2001) · Nature · doi:10.1038/35069000 · Cited by 1,610
Nanoconfinement controls stiffness, strength and mechanical toughness of β-sheet crystals in silk
Keten, S., Xu, Z., Ihle, B., & Buehler, M. J. (2010) · Nature Materials · doi:10.1038/nmat2704 · Cited by 1,391
Hu, X., Kaplan, D., & Cebe, P. (2006) · Macromolecules · doi:10.1021/ma0610109 · Cited by 1,251
The mechanical design of spider silks: from fibroin sequence to mechanical function
Gosline, J. M., Guerette, P. A., Ortlepp, C. S., & Savage, K. N. (1999) · Journal of Experimental Biology · doi:10.1242/jeb.202.23.3295 · Cited by 1,165
Surprising strength of silkworm silk
Shao, Z., & Vollrath, F. (2002) · Nature · doi:10.1038/418741a · Cited by 1,003
Structure of a protein superfiber: spider dragline silk.
Xu, M., & Lewis, R. V. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.18.7120 · Cited by 671
Molecular Orientation and Two-Component Nature of the Crystalline Fraction of Spider Dragline Silk
Simmons, A. H., Michal, C. A., & Jelinski, L. W. (1996) · Science · doi:10.1126/science.271.5245.84 · Cited by 632
Self-assembly of spider silk proteins is controlled by a pH-sensitive relay
Askarieh, G., Hedhammar, M., Nordling, K., Saenz, A., Casals, C., Rising, A., Johansson, J., & Knight, S. D. (2010) · Nature · doi:10.1038/nature08962 · Cited by 460
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Silk fibroin biomaterials for tissue regenerations
Kundu, B., Rajkhowa, R., Kundu, S. C., & Wang, X. (2013) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2012.09.043 · Cited by 1,391
Structures, mechanical properties and applications of silk fibroin materials
Koh, L.-D., Cheng, Y., Teng, C.-P., Khin, Y.-W., Loh, X.-J., Tee, S.-Y., Low, M., Ye, E., Yu, H.-D., Zhang, Y.-W., et al. (2015) · Progress in Polymer Science · doi:10.1016/j.progpolymsci.2015.02.001 · Cited by 1,241
Scaffolds for bone-tissue engineering
Lee, S. S., Du, X., Kim, I., & Ferguson, S. J. (2022) · Matter · doi:10.1016/j.matt.2022.06.003 · Cited by 375
Nanoconfinement of Spider Silk Fibrils Begets Superior Strength, Extensibility, and Toughness
Giesa, T., Arslan, M., Pugno, N. M., & Buehler, M. J. (2011) · Nano Letters · doi:10.1021/nl203108t · Cited by 274
Metadata
- Authors
- Du, N., Yang, Z., Liu, X. Y., Li, Y., & Xu, H. Y.
- Venue
- Advanced Functional Materials
- Publisher
- Wiley
- Published
- 2010-12-14
- Volume
- 21
- Issue
- 4
- Pages
- 772-778
- ISSN
- 1616-301X (ISSN-L)
- 1616-3028
- OpenAlex
- W2018653426
- Cited by
- 290
- References
- 25
- FWCI
- 3.66
- Type
- journal article
- Language
- en
- Open access
- closed
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