Journal
ACS NANO
Volume 6, Issue 3, Pages 1961-1969Publisher
AMER CHEMICAL SOC
DOI: 10.1021/nn300130q
Keywords
spider silk; collagen; mechanics; fibrils; toughness; finite; element; analysis
Categories
Funding
- Ministry for Foreign Affairs of Italy (Direzione Generale per la Promozione e la Cooperazione Culturale)
- MDEIE (Quebec)
- Fonds de la Recherche en Sante Quebec, Canada
- Canada Research Chairs program
- Natural Sciences and Engineering Research Council of Canada
- NIHR Biomedical Research Unit into Musculoskeletal Disease, Nuffield Orthopaedic Centre and University of Oxford, and Arthritis Research UK
- Cancer Research UK
- Versus Arthritis [18887] Funding Source: researchfish
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Spider silk is a fascinating natural composite material. Its combination of strength and toughness is unrivalled in nature, and as a result, it has gained considerable interest from the medical, physics, and materials communities. Most of this attention has focused on the one to tens of nanometer scale: predominantly the primary (peptide sequences) and secondary (beta sheets, helices, and amorphous domains) structure, with some insights into tertiary structure (the arrangement of these secondary structures) to describe the origins of the mechanical and biological performance. Starting with spider silk, and relating our findings to collagen fibrils, we describe toughening mechanisms at the hundreds of nanometer scale, namely, the fibril morphology and its consequences for mechanical behavior and the dissipation of energy. Under normal conditions, this morphology creates a nonslip fibril kinematics, restricting shearing between fibrils, yet allowing controlled local slipping under high shear stress, dissipating energy without bulk fracturing. This mechanism provides a relatively simple target for biomimicry and, thus, can potentially be used to increase fracture resistance in synthetic materials.
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