Precise correlation of macroscopic mechanical properties and microscopic structures of animal silks—using Antheraea pernyi silkworm silk as an example

2017 ◽  
Vol 5 (30) ◽  
pp. 6042-6048 ◽  
Author(s):  
Guangqiang Fang ◽  
Yuzhao Tang ◽  
Zeming Qi ◽  
Jinrong Yao ◽  
Zhengzhong Shao ◽  
...  

The structure of wild silkworm silk can be controlled by reeling rate, thus regulating its mechanical performance from close to spider dragline silk to domestic silkworm silk.

2010 ◽  
Vol 7 (53) ◽  
pp. 1709-1721 ◽  
Author(s):  
Sinan Keten ◽  
Markus J. Buehler

Spider silk is a self-assembling biopolymer that outperforms most known materials in terms of its mechanical performance, despite its underlying weak chemical bonding based on H-bonds. While experimental studies have shown that the molecular structure of silk proteins has a direct influence on the stiffness, toughness and failure strength of silk, no molecular-level analysis of the nanostructure and associated mechanical properties of silk assemblies have been reported. Here, we report atomic-level structures of MaSp1 and MaSp2 proteins from the Nephila clavipes spider dragline silk sequence, obtained using replica exchange molecular dynamics, and subject these structures to mechanical loading for a detailed nanomechanical analysis. The structural analysis reveals that poly-alanine regions in silk predominantly form distinct and orderly beta-sheet crystal domains, while disorderly regions are formed by glycine-rich repeats that consist of 3 1 -helix type structures and beta-turns. Our structural predictions are validated against experimental data based on dihedral angle pair calculations presented in Ramachandran plots, alpha-carbon atomic distances, as well as secondary structure content. Mechanical shearing simulations on selected structures illustrate that the nanoscale behaviour of silk protein assemblies is controlled by the distinctly different secondary structure content and hydrogen bonding in the crystalline and semi-amorphous regions. Both structural and mechanical characterization results show excellent agreement with available experimental evidence. Our findings set the stage for extensive atomistic investigations of silk, which may contribute towards an improved understanding of the source of the strength and toughness of this biological superfibre.


2007 ◽  
Vol 93 (12) ◽  
pp. 4425-4432 ◽  
Author(s):  
T. Vehoff ◽  
A. Glišović ◽  
H. Schollmeyer ◽  
A. Zippelius ◽  
T. Salditt

2019 ◽  
Vol 19 (3) ◽  
pp. 1970006 ◽  
Author(s):  
Kenjiro Yazawa ◽  
Ali D. Malay ◽  
Hiroyasu Masunaga ◽  
Keiji Numata

RSC Advances ◽  
2015 ◽  
Vol 5 (2) ◽  
pp. 1640-1647 ◽  
Author(s):  
J. Zhang ◽  
S. Du ◽  
A. Kafi ◽  
B. Fox ◽  
J. L. Li ◽  
...  

Both the physical and physiochemical properties of domestic and wild silkworm silk fibroin were studied, including surface energy and surface energy heterogeneity.


2021 ◽  
Author(s):  
Nobuaki Kono ◽  
Hiroyuki Nakamura ◽  
Masaru Mori ◽  
Yuki Yoshida ◽  
Rintaro Ohtoshi ◽  
...  

AbstractDragline silk of golden orb-weaver spiders (Nephilinae) is noted for its unsurpassed toughness, combining extraordinary extensibility and tensile strength, suggesting industrial application as a sustainable biopolymer material. To pinpoint the molecular composition of dragline silk and the roles of its constituents in achieving its mechanical properties, we report a multiomics approach combining high-quality genome sequencing and assembly, silk gland transcriptomics, and dragline silk proteomics of four Nephilinae spiders. We observed the consistent presence of the MaSp3B spidroin unique to this subfamily, as well as several non-spidroin SpiCE proteins. Artificial synthesis and combination of these components in vitro showed that the multicomponent nature of dragline silk, including MaSp3B and SpiCE, along with MaSp1 and MaSp2, is essential to realize the mechanical properties of spider dragline silk.


2016 ◽  
Vol 46 (6) ◽  
pp. 552-558 ◽  
Author(s):  
Haibo Zhang ◽  
Fengli Zhou ◽  
Xinglin Jiang ◽  
Mingle Cao ◽  
Shilu Wang ◽  
...  

2010 ◽  
Vol 2010 ◽  
pp. 1-8 ◽  
Author(s):  
Yaopeng Zhang ◽  
Hongxia Yang ◽  
Huili Shao ◽  
Xuechao Hu

The outstanding properties of spider dragline silk are likely to be determined by a combination of the primary sequences and the secondary structure of the silk proteins.Antheraea pernyisilk has more similar sequences to spider dragline silk than the silk from its domestic counterpart,Bombyx mori. This makes it much potential as a resource for biospinning spider dragline silk. This paper further verified its possibility as the resource from the mechanical properties and the structures of theA. pernyisilks prepared by forcible reeling. It is surprising that the stress-strain curves of theA. pernyifibers show similar sigmoidal shape to those of spider dragline silk. Under a controlled reeling speed of 95 mm/s, the breaking energy was1.04×105 J/kg, the tensile strength was 639 MPa and the initial modulus was 9.9 GPa. It should be noted that this breaking energy of theA. pernyisilk approaches that of spider dragline silk. The tensile properties, the optical orientation and theβ-sheet structure contents of the silk fibers are remarkably increased by raising the spinning speeds up to 95 mm/s.


Nanomaterials ◽  
2018 ◽  
Vol 8 (11) ◽  
pp. 918 ◽  
Author(s):  
Dan Tian ◽  
Chun-Hui He ◽  
Ji-Huan He

Electrospinning is now commercially used for the fabrication of nano/micro fibers. Compared with spider dragline silk, artificial fibers have poor mechanical properties. Unlike natural silk, which has a hierarchical structure with an approximate 3-fold symmetry, the molecular structure of spun fiber has neither folding nor orientation. To date, it is almost impossible to control molecule orientation during the spinning process. Here, we show that macromolecule orientation can be easily controlled using the laminar flow of fluid mechanics. A lasting laminar flow in a long needle can order macromolecules. We find that the orientation of macromolecules can greatly affect the morphology and mechanical properties of fibers. We expect our technology to be helpful for more sophisticated fabrication of fibers with ordered macromolecules and DNA-like twists.


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