2013
DOI: 10.1016/j.ijbiomac.2013.02.018
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Microstructural change of degummed Bombyx mori silk: An in situ stretching wide-angle X-ray-scattering study

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Cited by 16 publications
(13 citation statements)
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“…This resulted in crystallite dimensions of 3, 4, and 5 nm in the a, b , and c axes, respectively. 25 Azimuthal broadening of the crystalline reflections is indicative of variance in alignment of the crystalline fraction with respect to the fiber axis. Hermans orientation factor of the crystalline fraction, f c , was calculated to be 0.93, from the FWHM of radial integration at 4.3 Å −1 where f c = (3(cos 2 Φ )−1)/2 and Φ is the angle between the c axis of the nanocrystallite and the fiber axis.…”
Section: Resultsmentioning
confidence: 99%
See 1 more Smart Citation
“…This resulted in crystallite dimensions of 3, 4, and 5 nm in the a, b , and c axes, respectively. 25 Azimuthal broadening of the crystalline reflections is indicative of variance in alignment of the crystalline fraction with respect to the fiber axis. Hermans orientation factor of the crystalline fraction, f c , was calculated to be 0.93, from the FWHM of radial integration at 4.3 Å −1 where f c = (3(cos 2 Φ )−1)/2 and Φ is the angle between the c axis of the nanocrystallite and the fiber axis.…”
Section: Resultsmentioning
confidence: 99%
“…Studies on spider dragline silk fibers show that the crystallinity content ranges from about 30% ( Nephila clavipes ) to 40% ( Latrodectus hesperus ), 23,24 while fibers from the domesticated silkworm are typically higher, in the range of 40–60% crystallinity. 25,26 The crystalline fractions arise mainly from repeated sequences, thus the primary protein sequence for webspinner silks should yield predictive power; protein secondary structure within spider dragline silk fibers has been shown to correlate quantitatively with silk primary protein sequences. 24,27 With the exception of short C-terminal domains, the protein sequences of many embiopteran silks are virtually entirely composed of repetitive motifs, which likely adopt a β-sheet structure.…”
Section: Introductionmentioning
confidence: 99%
“…The intra and intermolecular hydrogen bond network provide strength and tensile strength to the biopolymer, while amorphous regions provide flexibility and elasticity [29]. In the literature, there is great variability in the sizes reported for these crystals [30][31][32][33]. To illustrate the size of these, reference can be made to X-ray diffraction measurements and low voltage transmission electron microscopy performed by Drummy et al [30].…”
Section: Figurementioning
confidence: 99%
“…Natural biopolymers are similar to both biological macromolecules present and metabolized in the biological environment 1 and the extracellular matrix, including collagen, gelatin, alginate, chitosan, hyaluronic acid, and silk fibroin (SF), which have shown high applicability for wound healing. Among such biopolymers, SF is a fibrous protein extracted from silkworm cocoons of Bombyx mori species and whose molecular structure is composed of hydrophilic and hydrophobic groups represented by α‐helix and β‐sheet secondary structures, respectively 2 . Those structures enable the obtaining of materials of specific properties (amorphous or crystalline characteristics), since, depending on the type of chemical and/or physical stimulus, the α‐helix structure can be converted into a β‐sheet one (crystalline domains or the so‐called ordered domains).…”
Section: Introductionmentioning
confidence: 99%
“…Several organic solvents are used for the obtaining of a stable solution of SF, although formic acid has excelled in the production of fibroin films and fibers 1–4 . According to Um et al, 20 the solubilization of fibroin in formic acid leads to a transparent solution that neither aggregates, nor precipitates after a long storage period.…”
Section: Introductionmentioning
confidence: 99%