Chemical, structural and thermal properties of Gonometa postica silk fibroin, a potential biomaterial

Mhuka, Vimbai; Dube, Simiso; Nindi, Mathew Muzi

doi:10.1016/j.ijbiomac.2012.09.010

Cited by 28 publications

(21 citation statements)

References 39 publications

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“…With such a variety of silk, it is not surprising that its molecular composition and structure can vary among the different species. SF of B. mori, the african wild silk moth Gonometa postica and G. rufobrunnea were compared amongst each other and revealed a significantly higher amount of polar (serine), acidic (aspartic acid) and basic (arginine) amino acids in Gonometa SF which can influence cell attachement and also alter chemical reacitivty for side chain modifications [44]. Indian tropical tasar silk of Antheraea mylitta or chinese oak tasar silk of A. pernyi, possess Arginine-glycine-aspartic acid (RGD) motifs in their amino acid sequences which is known to mediate cell attachment (reference: GenBank: AY136274.1, Submitted (on JUL-2002) to the EMBL/GenBank/DDBJ databases).…”

Section: Structure and Mechanical Propertiesmentioning

confidence: 99%

Silk fibroin as biomaterial for bone tissue engineering

et al. 2016

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Silk fibroin is a natural biomaterial with remarkable biomedical and mechanical properties which make it favorable for a broad range of bone tissue engineering applications. It can be processed into different scaffold forms, combined synergistically with other biomaterials to form composites and chemically modified which provides a unique toolbox and allows silk fibroin scaffolds to be tailored to specific applications. This review discusses and summarizes recent advancements in processing silk fibroin, focusing on different fabrication and functionalization methods and their application to grow bone tissue in vitro and in vivo. Potential areas for future research, current challenges, uncertainties and gaps in knowledge are highlighted.

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Section: Structure and Mechanical Propertiesmentioning

confidence: 99%

Silk fibroin as biomaterial for bone tissue engineering

et al. 2016

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“…Also, it occurs from a broad endothermic transition ascribed to the thermal decomposition of Table 2 Average values and standard deviation of the mechanical properties and real density of the silk fiber threads obtained from the different supplemental conditions silk fibers with oriented b-sheet crystalline structure [47]. The shoulder peaks at around 500 and 600°C for all conditions are associated with the mass loss due to the decomposition of the fibroin molecules [39]. For the control sample (from untreated leaves), the decomposition of the fibroin occurred with the shoulder peak at around 500°C and with the second one at around 550°C (Fig.…”

Section: Ft-ir Resultsmentioning

confidence: 99%

“…5. The peak observed at 20.2°c orresponds to silk II structure (b-sheet crystallinity) [39]; the peaks appearing at *10°and 28°have been also reported to be characteristic of silk fibers [40,41].…”

Section: X-ray Diffractionmentioning

confidence: 92%

Impact of different silkworm dietary supplements on its silk performance

et al. 2014

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This study aims to evaluate the effect of silkworm larva (Bombyx mori) diet supplementation with two amino acids (threonine and valine) on the cocoon production and on the structural and mechanical properties of the silk produced. Negligible morphological differences were observed in the silk fiber threads from silkworm larvae supplemented with the tested amino acids. Higher production (yield) of silk was obtained using threonine in the diet of the silkworm. The treatments with threonine have increased the limit of proportionality, tensile strength, toughness, and maximum deformation of the thread of silk fibers. No significant increment in these properties was observed due to the increase in the threonine content. The treatments with valine led to lower increase in tensile strength and toughness. The real density of the silk has decreased with the use of supplements. The present study contributes to engineering of advanced silk materials, which should be attractive candidates for multipurpose applications.

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“…Considering the amino acid compositions, all silk fibroin films had common amino acids, for example glycine, alanine, and serine. These three amino acids have the smallest side chains, allowing for regular packing in the formation of the beta sheet structure of silk fibroin . The total percentage of hydrophilic amino acid groups of K1 was slightly higher than that of K8, but that of NN silk fibroin was more hydrophobic.…”

Section: Discussionmentioning

confidence: 98%

Physico‐chemical properties and in vitro response of silk fibroin from various domestic races

et al. 2014

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In this study, the characteristics of silk fibroin films obtained from regenerated aqueous silk fibroin solution of various races were evaluated. Three races based on original sources of silkworms were selected: Nangnoi-Sisaket 1 (NN), Nakhon Ratchasima 1 (K1), and Nakhon Ratchasima 2 (K8). The Tg and Td of silk fibroin films were around 147-156°C and 277-279°C, respectively. FTIR result revealed that all silk fibroin films had beta sheet conformation. K1 and K8 films were found to be more hydrophilic than NN film. From in vitro tests using L929 mouse fibroblast and rat bone marrow-derived stem cells (rMSCs), the cell attachment was slightly greater on K1 film than the other two films. The enhanced cell growth on K1 film might be related to its slightly high hydrophilicity and the higher content of serine. The result of osteogenic differentiation test showed that alkaline phosphatase and deposited mineral of rMSCs were higher on all silk fibroin films than on tissue culture plate. K1 film tended to promote osteogenic differentiation of rMSCs to a higher extent than NN and K8 films. K1 silk fibroin film exhibited a higher potential to support cell attachment, proliferation, and differentiation than other two films.

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Chemical, structural and thermal properties of Gonometa postica silk fibroin, a potential biomaterial

Cited by 28 publications

References 39 publications

Silk fibroin as biomaterial for bone tissue engineering

Silk fibroin as biomaterial for bone tissue engineering

Impact of different silkworm dietary supplements on its silk performance

Physico‐chemical properties and in vitro response of silk fibroin from various domestic races

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