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Abstract Biomaterials with outstanding mechanical properties, including spider silk, wood, and cartilage, often feature an oriented nanofibrillar structure. The orientation of nanofibrils gives rise to a significant mechanical anisotropy, which is extremely challenging to characterize, especially for microscopically small or inhomogeneous samples. Here, a technique utilizing atomic force microscope indentation at multiple points combined with finite element analysis to sample the mechanical anisotropy of a thin film in a microscopically small area is reported. The system studied here is the tape‐like silk of the Chilean recluse spider, which entirely consists of strictly oriented nanofibrils giving rise to a large mechanical anisotropy. The most detailed directional nanoscale structure–property characterization of spider silk to date is presented, revealing the tensile and transverse elastic moduli as 9 and 1 GPa, respectively, and the binding strength between silk nanofibrils as 159±13 MPa. Furthermore, based on this binding strength, the nanofibrils’ surface energy is derived as 37 mJ m−2, and concludes that van der Waals forces play a decisive role in interfibrillar binding. Due to its versatility, this technique has many potential applications, including early disease diagnostics, as underlying pathological conditions can alter the local mechanical properties of tissues.
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Protein secondary structure in spider silk nanofibrils
Abstract Nanofibrils play a pivotal role in spider silk and are responsible for many of the impressive properties of this unique natural material. However, little is known about the internal structure of these protein fibrils. We carry out polarized Raman and polarized Fourier-transform infrared spectroscopies on native spider silk nanofibrils and determine the concentrations of six distinct protein secondary structures, including β-sheets, and two types of helical structures, for which we also determine orientation distributions. Our advancements in peak assignments are in full agreement with the published silk vibrational spectroscopy literature. We further corroborate our findings with X-ray diffraction and magic-angle spinning nuclear magnetic resonance experiments. Based on the latter and on polypeptide Raman spectra, we assess the role of key amino acids in different secondary structures. For the recluse spider we develop a highly detailed structural model, featuring seven levels of structural hierarchy. The approaches we develop are directly applicable to other proteinaceous materials.
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- PAR ID:
- 10381723
- Publisher / Repository:
- Nature Publishing Group
- Date Published:
- Journal Name:
- Nature Communications
- Volume:
- 13
- Issue:
- 1
- ISSN:
- 2041-1723
- Format(s):
- Medium: X
- Sponsoring Org:
- National Science Foundation
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