Preparation and physical properties of antheraea yamamai/Bombyx mori silk fibroin blending film

Lv, Linlin; Wei, Yanqiong; Wang, Jiannan; Li, Mingzhong; Zhao, Haipeng; Liu, Guiyang; Lu, Qiang

doi:10.1109/bmei.2011.6098528

Cited by 3 publications

(4 citation statements)

References 34 publications

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“…24,25 The specic nanostructure of BSF existed, and the layer structure of TSF disappeared in the blend lms. Furthermore, the morphological phase separation was not observed, which had been reported in the BSF/TSF, 26 and in the TSF/carboxymethyl chitosan blend lms prepared using water as a co-solvent. 27 The possible reason was that formic acid was an excellent solvent for silk broin dissolution and regeneration, 28 but water was just a temporary solvent for silk broin in which gel formed easily.…”

Section: Morphologymentioning

confidence: 65%

A novel method to prepare tussah/Bombyx mori silk fibroin-based films

Yang

Wang

et al. 2018

RSC Adv.

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The possibility of using silk fibroin in biomaterials for tissue engineering is a subject of broad interest. In this study, Bombyx mori/tussah silk fibroin (BSF/TSF) blend films were prepared by solution casting using CaCl 2 / formic acid as a co-solvent and water as a rinse solvent. The morphology, crystallinity, thermal resistance, mechanical properties and water contact angle of the blend films as well as the biocompatibility were investigated. The BSF/TSF blend films displayed a smooth surface and specific nanostructure in their cross-section, originating from the nanofibril-preservation during fibroin dissolution. The water rinse process induced the formation of a stable b-sheet structure. The BSF film showed superior mechanical properties to the TSF film, and the blending with TSF led to a significant reduction in the strength and elasticity of blend films. However, adding the TSF component could regulate the hydrophilic properties and enhance cell growth on the blend films. The BSF/TSF blend films with specific nanostructure, stable secondary structure, appropriate mechanical properties, and good biocompatibility, are promising candidates for application in regenerative medicine.

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Section: Morphologymentioning

confidence: 65%

A novel method to prepare tussah/Bombyx mori silk fibroin-based films

Yang

Wang

et al. 2018

RSC Adv.

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“…The silk fibroin's crystallinity is affected by β-sheet composition. The intense peaks on the XRD curves of degummed fiber at 16.45° and 20.31° indicate an intense β-sheet structure [21]. In regenerated fibroin, the β-sheet high-crystalline structure was noticed, with a diffraction peak at 20.95° [22].…”

Section: Discussionmentioning

confidence: 98%

“…The XRD patterns of both degummed silk fibroin (SF) and RSF were examined to detect the variations in the crystalline structure. The XRD pattern helps to predict and confirm the α-helix and β-sheet structure with Cu Kα radiation [21].…”

Section: X-ray Diffractionmentioning

confidence: 99%

Biocompatibility of hydrophilic regenerated Antheraea mylitta silk fibroin

Dixit¹,

Gasti²,

Sherapura³

et al. 2023

J App Biol Biotech

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Silk, a natural biopolymer, is used for both textile and biomedical applications. Natural biopolymers are currently being used in various fields such as tissue engineering, wound healing, and food packaging based on their intrinsic qualities of safety, biocompatibility, and biodegradability, which make them the material of choice. Silk fibroin proteins from the Antheraea mylitta wild silkworm are the least studied in the field of biomaterials. The β-sheet structures found in non-mulberry silk fibroin protein improve its mechanical properties. The present study was undertaken to regenerate water-soluble A. mylitta silk fibroin to improve its applications and enhance fabrication efficiency. The silk fibroin was regenerated by dissolving degummed silk fibers in calcium nitrate tetrahydrate salt at 100°C for 3 h. The biophysical characterization of regenerated silk fibroin was carried out by X-ray diffraction, scanning electron microscope, Therapeutic Goods Administration, Fourier-transform infrared spectroscopy, and differential scanning calorimetry, confirming the indigenous aspects of the "regenerated silk fibroin (RSF)". CD spectra were employed to track α-helix to β-sheet conformational transition changes in RSF. MTT assays using NIH3T3 fibroblast cells revealed that the RSF exhibited no toxicity and resulted in the proliferation of cells.

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“…However, BMSF does not contain RGD or any other known ligand peptide motif [ 2 , 23 , 24 , 25 ]. On the other hand, the fibroins isolated from the silk produced by the larvae of wild silkmoths in the family Saturniidae , genus Antheraea , such as A. pernyi , A. mylitta and A. yamamai , which do not feed on mulberry leaves, contain RGD domains in their structure [ 2 , 26 , 27 , 28 , 29 , 30 , 31 , 32 ], and thus are perceived to be more suitable as substrata for cells. The absence in BMSF of adhesion peptide domains makes it rather difficult to explain its cell-adhesive properties, which have been indeed proved suitable for growing a variety of cells.…”

Section: Introductionmentioning

confidence: 99%

Incorporation of Exogenous RGD Peptide and Inter-Species Blending as Strategies for Enhancing Human Corneal Limbal Epithelial Cell Growth on Bombyx mori Silk Fibroin Membranes

Bray

Suzuki

Harkin

2013

JFB

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While fibroin isolated from the cocoons of domesticated silkworm Bombyx mori supports growth of human corneal limbal epithelial (HLE) cells, the mechanism of cell attachment remains unclear. In the present study we sought to enhance the attachment of HLE cells to membranes of Bombyx mori silk fibroin (BMSF) through surface functionalization with an arginine-glycine-aspartic acid (RGD)-containing peptide. Moreover, we have examined the response of HLE cells to BMSF when blended with the fibroin produced by a wild silkworm, Antheraea pernyi, which is known to contain RGD sequences within its primary structure. A procedure to isolate A. pernyi silk fibroin (APSF) from the cocoons was established, and blends of the two fibroins were prepared at five different BMSF/APSF ratios. In another experiment, BMSF surface was modified by binding chemically the GRGDSPC peptide using a water-soluble carbodiimide. Primary HLE were grown in the absence of serum on membranes made of BMSF, APSF, and their blends, as well as on RGD-modified BMSF. There was no statistically significant enhancing effect on the cell attachment due to the RGD presence. This suggests that the adhesion through RGD ligands may have a complex mechanism, and the investigated strategies are of limited value unless the factors contributing to this mechanism become better known.

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Preparation and physical properties of antheraea yamamai/Bombyx mori silk fibroin blending film

Cited by 3 publications

References 34 publications

A novel method to prepare tussah/Bombyx mori silk fibroin-based films

A novel method to prepare tussah/Bombyx mori silk fibroin-based films

Biocompatibility of hydrophilic regenerated Antheraea mylitta silk fibroin

Incorporation of Exogenous RGD Peptide and Inter-Species Blending as Strategies for Enhancing Human Corneal Limbal Epithelial Cell Growth on Bombyx mori Silk Fibroin Membranes

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