Silk Fiber — Molecular Formation Mechanism, Structure- Property Relationship and Advanced Applications

Liu, Xinfang; Zhang, Ke‐Qin

doi:10.5772/57611

Cited by 38 publications

(50 citation statements)

References 194 publications

(243 reference statements)

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“…The d ‐spacings for each peak are calculated by using the d = 2π / q formula and are d 1 = 4.69 nm , d 2 = 0.96 nm, d 3 = 0.42 nm , d 4 = 0.36 nm, d 5 = 0.27 nm and d 6 = 0.22 nm, respectively. The d ‐spacings observed at 0.42, 0.36, 0.27 and 0.22 nm correspond to the distance between β‐strands and the primary structure, in particular the silk II crystalline spacings, the distance at 0.96 nm corresponds to the inter‐sheet distance between β‐sheets and the distance at 4.69 nm corresponds to the size of the β‐sheets in the lateral direction . In cellulose powder, three distinct spacings are observed.…”

Section: Resultsmentioning

confidence: 97%

Morphology and ionic conductivity relationship in silk/cellulose biocomposites

Blessing

Trout

Morales

et al. 2019

Polymer International

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The relationship between morphology and the ionic conductivity of polysaccharide–protein bio‐electrolyte membranes is explored in this study. Structural proteins and polysaccharides form hydrophobic and electrostatic interactions, and the resulting matrices can exhibit novel and useful properties. However, transforming these natural biomacromolecules from their native state to a more usable form is challenging. The structural, morphological, thermal, mechanical and electrical properties of biomaterials composed of microcrystalline cellulose and Bombyx mori silk when regenerated together using ionic liquids and various coagulation agents were investigated using a diverse set of techniques including Fourier transform infrared spectroscopy, SEM, TGA, DSC, X‐ray scattering, AFM‐based nanoindentation and dielectric relaxation spectroscopy. The surface topography of the films reveals morphological changes with varying coagulation agents and ionic liquids. It was found that the thermal and mechanical properties were dependent on intermolecular interactions dictated by the type of ionic liquid used during the coagulation process. X‐ray scattering provided information on how the cellulose crystallinity varied with coagulation agent. Specifically, samples coagulated with hydrogen peroxide showed an increase in cellulose crystallinity impacting properties such as elasticity, hardness and ionic conductivity of the biocomposites. In addition, the results revealed a strong correlation between β‐sheet content and ionic conductivity and cellulose crystallinity. The results provided evidence that the ionic conductivity is dependent on protein β‐sheet content and cellulose crystallinity. © 2019 Society of Chemical Industry

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Section: Resultsmentioning

confidence: 97%

Morphology and ionic conductivity relationship in silk/cellulose biocomposites

Blessing

Trout

Morales

et al. 2019

Polymer International

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“…The mechanism by which soluble silk proteins form an insoluble silk thread is reviewed by Liu and Zhang [20]. The fibroin is secreted into the glandular lumen in solution form with approximately 15% of protein, migrating to the middle region where it is surrounded by the sericin.…”

Section: Sericin Synthesis and Silk Gland Morphologymentioning

confidence: 99%

“…While spinning, the proteins flow through the anterior silk gland duct, where excess water and ions are absorbed, and the crystalline liquid solution solidifies gradually converting into a solid filament. Furthermore, a specific and continuous movement of B. mori head during spinning also acts on the orientation of protein molecules in the silk thread, and as the silk proteins aggregate and crystallize, they become more hydrophobic, inducing the loss of water on the surface of the thread [20]. …”

Section: Sericin Synthesis and Silk Gland Morphologymentioning

confidence: 99%

Silkworm Sericin: Properties and Biomedical Applications

Kunz

Brancalhão

Ribeiro

et al. 2016

BioMed Research International

313

261

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Silk sericin is a natural polymer produced by silkworm, Bombyx mori, which surrounds and keeps together two fibroin filaments in silk thread used in the cocoon. The recovery and reuse of sericin usually discarded by the textile industry not only minimizes environmental issues but also has a high scientific and commercial value. The physicochemical properties of the molecule are responsible for numerous applications in biomedicine and are influenced by the extraction method and silkworm lineage, which can lead to variations in molecular weight and amino acid concentration of sericin. The presence of highly hydrophobic amino acids and its antioxidant potential make it possible for sericin to be applied in the food and cosmetic industry. The moisturizing power allows indications as a therapeutic agent for wound healing, stimulating cell proliferation, protection against ultraviolet radiation, and formulating creams and shampoos. The antioxidant activity associated with low digestibility of sericin that expands the application in the medical field, such as antitumour, antimicrobial and anti-inflammatory agent, anticoagulant, acts in colon health, improving constipation and protects the body from obesity through improved plasma lipid profile. In addition, the properties of sericin allow its application as a culture medium and cryopreservation, in tissue engineering and for drug delivery, demonstrating its effective use, as an important biomaterial.

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“…From previous spectroscopic studies on the secondary structure of silk fibers, it has been recognized that silk fibers mainly comprise a crystalline Silk II structure, which is mainly composed of a β-sheet structure. [5][6][7][8][9][10][11][27][28][29] In general, β-sheet-rich globular proteins give a negative couplet that comprises a strong right-handed optically active band at around 1630 cm -1 as a main part and a weak left-handed band at around 1660 cm -1 as a minor part. 16 It has been also reported that the minor band was not observed.…”

Section: Resultsmentioning

confidence: 99%

“…4 Thus, much attention has been focused on the mechanism of the structural transition from liquid silk to silk fibers not only to understand the structural origin of the expression of their excellent mechanical properties and biocompatibility but also to develop materials that are more advanced than silk fibers. [5][6][7][8][9][10][11] For the spectroscopic study of the mechanism, silk fibroin concentrated aqueous solutions that are formed by the lysis of silk fibers in LiBr or CaCl2/C2H5OH solutions at high temperatures, called regenerated silk fibroin solutions, have been used. [6][7][8][9]11 By electronic circular dichroism (ECD) and infrared (IR) absorption measurements and X-ray scattering and NMR ones under shear, it was observed that regenerated silk fibroin solutions adopted a random-coil structure and they were converted into crystalline fibers with a Silk II structure, which mainly comprised a β-sheet structure.…”

Section: Introductionmentioning

confidence: 99%

Structural Transition of Bombyx mori Liquid Silk Studied with Vibrational Circular Dichroism Spectroscopy

et al. 2015

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7As another intermediate structure, an α-helix-rich crystalline Silk I structure was also observed by X-ray scattering 2015 © The Japan Society for Analytical Chemistry † To whom correspondence should be addressed. Agriculture and Technology, Koganei, Japan We investigated the structural transition from liquid silk to silk fibers with vibrational circular dichroism spectroscopy. Liquid silk showed a major right-handed optically active band at around 1650 cm -1 and a minor one at around 1680 cm -1 . The former disappeared over time, while the intensity in the latter increased. With the former wavenumber, liquid silk mainly adopted a random-coil structure. In contrast, the latter may reflect an intermediate structure in the transition. Furthermore, two right-handed bands at around 1630 and 1660 cm -1 appeared with the disappearance of the major band, and then the wavenumber of the former shifted to around 1620 cm -1 . The shift results from the decrease in the frequency of the CO stretching mode due to the stacking of the β-sheet that comprises fibers. The band at 1660 cm -1 may reflect another intermediate structure due to its strong correlation with that at 1620 cm -1 in terms of their temporal change in intensity.

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Silk Fiber — Molecular Formation Mechanism, Structure- Property Relationship and Advanced Applications

Cited by 38 publications

References 194 publications

Morphology and ionic conductivity relationship in silk/cellulose biocomposites

Morphology and ionic conductivity relationship in silk/cellulose biocomposites

Silkworm Sericin: Properties and Biomedical Applications

Structural Transition of Bombyx mori Liquid Silk Studied with Vibrational Circular Dichroism Spectroscopy

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