Nanoconfinement of Spider Silk Fibrils Begets Superior Strength, Extensibility, and Toughness. Giesa, T., Arslan, M., Pugno, N. M., & Buehler, M. J. Nano Letters, 11(11):5038–5046, November, 2011. Publisher: American Chemical Society![Nanoconfinement of Spider Silk Fibrils Begets Superior Strength, Extensibility, and Toughness [link]](https://bibbase.org/img/filetypes/link.svg "link")
Paper doi abstract bibtex Silk is an exceptionally strong, extensible, and tough material made from simple protein building blocks. The molecular structure of dragline spider silk repeat units consists of semiamorphous and nanocrystalline β-sheet protein domains. Here we show by a series of computational experiments how the nanoscale properties of silk repeat units are scaled up to create macroscopic silk fibers with outstanding mechanical properties despite the presence of cavities, tears, and cracks. We demonstrate that the geometric confinement of silk fibrils to diameters of 50 ± 30 nm is critical to facilitate a powerful mechanism by which hundreds of thousands of protein domains synergistically resist deformation and failure to provide enhanced strength, extensibility, and toughness at the macroscale, closely matching experimentally measured mechanical properties. Through this mechanism silk fibers exploit the full potential of the nanoscale building blocks, regardless of the details of microscopic loading conditions and des...
@article{giesa_nanoconfinement_2011,
title = {Nanoconfinement of {Spider} {Silk} {Fibrils} {Begets} {Superior} {Strength}, {Extensibility}, and {Toughness}},
volume = {11},
issn = {1530-6984},
url = {https://pubs.acs.org/doi/10.1021/nl203108t},
doi = {10.1021/nl203108t},
abstract = {Silk is an exceptionally strong, extensible, and tough material made from simple protein building blocks. The molecular structure of dragline spider silk repeat units consists of semiamorphous and nanocrystalline β-sheet protein domains. Here we show by a series of computational experiments how the nanoscale properties of silk repeat units are scaled up to create macroscopic silk fibers with outstanding mechanical properties despite the presence of cavities, tears, and cracks. We demonstrate that the geometric confinement of silk fibrils to diameters of 50 ± 30 nm is critical to facilitate a powerful mechanism by which hundreds of thousands of protein domains synergistically resist deformation and failure to provide enhanced strength, extensibility, and toughness at the macroscale, closely matching experimentally measured mechanical properties. Through this mechanism silk fibers exploit the full potential of the nanoscale building blocks, regardless of the details of microscopic loading conditions and des...},
number = {11},
urldate = {2019-03-04},
journal = {Nano Letters},
author = {Giesa, Tristan and Arslan, Melis and Pugno, Nicola M. and Buehler, Markus J.},
month = nov,
year = {2011},
note = {Publisher: American Chemical Society},
keywords = {Spider silk, coarse-grain model, deformation, geometric confinement, materiomics, mechanical properties, molecular simulation},
pages = {5038--5046},
}
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