Facile and rapid ruthenium mediated photo-crosslinking of Bombyx mori silk fibroin

Whittaker, Jasmin L.; Choudhury, Namita Roy; Dutta, Naba K.; Zannettino, Andrew C.W.

doi:10.1039/c4tb00698d

Cited by 89 publications

(124 citation statements)

References 41 publications

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“…As the NaNO 3 concentration increased, typical nitrotyrosine peaks increased at 274 nm and 356 nm [22], indicating that the tyrosine reacted to the NaNO 3 , and that the nitration of the SF modified the tyrosine to nitrotyrosine. This finding is consistent with the results of the amino acid analysis of the SF gel [23]. …”

Section: Resultssupporting

confidence: 93%

Gelation Behaviors and Mechanism of Silk Fibroin According to the Addition of Nitrate Salts

Kim

Yoon

et al. 2016

IJMS

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Silk fibroin (SF) is a typical fibrous protein that is secreted by silkworms and spiders. It has been used in a variety of areas, and especially for tissue-engineering scaffolds, due to its sound processability, mechanical properties, biodegradability, and biocompatibility. With respect to gelation, the SF gelation time is long in aqueous solutions, so a novel approach is needed to shorten this time. The solubility of regenerated SF is sound in formic acid (FA), which is a carboxylic acid of the simplest structure. In this study, SF was dissolved in formic acid, and the addition of salts then induced a rapid gelation that accompanied a solution-color change. Based on the gelation behaviors of the SF solution according to different SF and salt concentrations, the gelation mechanism was investigated.

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Section: Resultssupporting

confidence: 93%

Gelation Behaviors and Mechanism of Silk Fibroin According to the Addition of Nitrate Salts

Kim

Yoon

et al. 2016

IJMS

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“…11 This reaction is also time-consuming. Ruthenium-mediated photo cross-linking of SF was reported by Whittaker et al 5 The mechanism is based on tyrosine and is rapid, but additive electron acceptors such as ammonium persulfate have some cytotoxicity. Therefore, it would be extremely important and useful to find a rapid and simple cross-linking method to develop chemically cross-linked SF hydrogels (SF C-gel).…”

Section: Introductionmentioning

confidence: 99%

Chemically cross-linked silk fibroin hydrogel with enhanced elastic properties, biodegradability, and biocompatibility

Kim¹,

Park²

2016

IJN

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In this study, the synthesis of silk fibroin (SF) hydrogel via chemical cross-linking reactions of SF due to gamma-ray (γ-ray) irradiation was investigated, as were the resultant hydrogel’s properties. Two different hydrogels were investigated: physically cross-linked SF hydrogel and chemically cross-linked SF hydrogel irradiated at different doses of γ-rays. The effects of the irradiation dose and SF concentration on the hydrogelation of SF were examined. The chemically cross-linked SF hydrogel was compared with the physically cross-linked one with regard to secondary structure and gel strength. Furthermore, the swelling behavior, crystallinity, and biodegradation of the SF hydrogels were characterized. To assay cell proliferation, the cell viability of human mesenchymal stem cells on the lyophilized SF hydrogel scaffolds was evaluated, and no significant cytotoxicity against human mesenchymal stem cells was observed.

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“…Recently, Whittaker et al . developed a photocrosslinkable hydrogel composed of Rec1-resilin and regenerated silk fibroin [56,57]. This combination of Rec1 with high elasticity and water uptake with silk with high strength provides an opportunity to design materials with a range of properties that could emulate tropoelastin-silk successes but with an entirely arthropod-protein based solution.…”

Section: Introductionmentioning

confidence: 99%

Elastic proteins and elastomeric protein alloys

Aghaei-Ghareh-Bolagh

Mithieux

Weiss

2016

Current Opinion in Biotechnology

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The elastomeric proteins elastin and resilin have been used extensively in the fabrication of biomaterials for tissue engineering applications due to their unique mechanical and biological properties. Tropoelastin is the soluble monomer component of elastin. Tropoelastin and resilin are both highly elastic with high resilience, substantial extensibility, high durability and low energy loss, which makes them excellent candidates for the fabrication of elastic tissues that demand regular and repetitive movement like the skin, lung, blood vessels, muscles and vocal folds. Combinations of these proteins with silk fibroin further enhance their biomechanical and biological properties leading to a new class of protein alloy materials with versatile properties. In this review, the properties of tropoelastin- and resilin-based biomaterials with and without silk are described in concert with examples of their applications in tissue engineering.

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Facile and rapid ruthenium mediated photo-crosslinking of Bombyx mori silk fibroin

Cited by 89 publications

References 41 publications

Gelation Behaviors and Mechanism of Silk Fibroin According to the Addition of Nitrate Salts

Gelation Behaviors and Mechanism of Silk Fibroin According to the Addition of Nitrate Salts

Chemically cross-linked silk fibroin hydrogel with enhanced elastic properties, biodegradability, and biocompatibility

Elastic proteins and elastomeric protein alloys

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