Silk fibroin: Structural implications of a remarkable amino acid sequence

Zhou, Cong‐Zhao; Confalonieri, Fabrice; Jacquet, Michel; Perasso, Roland; Li, Zhengang; Janin, Joël

doi:10.1002/prot.1078

Cited by 650 publications

(757 citation statements)

References 9 publications

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“…[104,107] It is a protein with a secondary molecular structure in the form of a beta-sheet that combines well with graphene. [17,108] SF has so far been produced in the form of films, fibers, electrospun mats, and 3D porous scaffolds.…”

Section: Sfmentioning

confidence: 99%

Graphene Oxide/Polymer‐Based Biomaterials

2017

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Since its discovery in 2004, derivatives of graphene have been developed and heavily investigated in the field of tissue engineering. Among the most extensively studied forms of graphene, graphene oxide (GO), and GO/ polymer-based nanocomposites have attracted great attention in various forms such as films, 3D porous scaffolds, electrospun mats, hydrogels, and nacre-like structures. In this review, the most actively investigated GO/ polymer nanocomposites are presented and discussed, these nanocomposites are based on chitosan, cellulose, starch, alginate, gellan gum, poly(vinyl alcohol) (PVA), poly(acrylamide), poly(e-caprolactone) (PCL), poly(lactic acid) (PLLA), poly(lactide-co-glycolide) (PLGA), gelatin, collagen, and silk fibroin (SF). The biological and mechanical performance of such nanocomposites are comprehensively scrutinized and ongoing research questions are addressed. The analysis of the literature reveals overall the great potential of GO/ polymer nanocomposites in tissue engineering strategies and indicates also a series of challenges requiring further research efforts.

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Section: Sfmentioning

confidence: 99%

Graphene Oxide/Polymer‐Based Biomaterials

2017

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“…The β-sheet-forming motif consists of oligo(lalanine) with a residue number ranging from 5 to 14 in the silks of spiders and some silkworms [11,[97][98][99] or a GAGAGX (G: glycine, A: alanine, and X: serine, glutamine, or tyrosine) tandem sequence in the silk of Bombyx mori silkworm. [100][101][102] The β-sheet-forming motif in the silk of spiders and some silkworms consists of only alanine residues and is therefore readily accessible by chemoenzymatic polymerization. PolyAla was synthesized by the papain-catalyzed polymerization of l-alanine ethyl ester.…”

Section: Hydrophobic Polypeptides For Structural Materialsmentioning

confidence: 99%

Chemoenzymatic Synthesis of Polypeptides for Use as Functional and Structural Materials

Tsuchiya

Numata

2017

Macromolecular Bioscience

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Polypeptides inspired by the natural functional and structural proteins present in living systems are promising materials for various fields in terms of their versatile functionality and physical properties. Designing and synthesizing mimetic sequences of specific peptide motifs in proteins are important for exploring the functionality of natural proteins. Chemoenzymatic polymerization, which utilizes aminolysis (i.e., the reverse reaction of hydrolysis catalyzed by proteases), is a useful technique for synthesizing artificial polypeptide materials and has several advantages, including facile synthesis protocols, environmental friendliness, scalability, and atom economy. In this review, recent progress in chemoenzymatic polypeptide synthesis for the production of functional and structural materials for various applications is summarized in conjunction with the current status of technical challenges in the field.

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Section: Introductionmentioning

confidence: 99%

“…Silk fibroin is a natural fibrous protein with a semicrystalline structure and it consists of heavy chain (390 kDa), light chain (25 kDa) and glycoprotein. Each polypeptides linked by disulfide bond (Zhou et al, 2001).Especially, fibroin as the main component of silk protein has found diverse applications in the biomedical field, which has a strong tensile strength, biodegradability and biocompatibility (Horan et al, 2005;Meinel et al, 2005). Hence, many researchers select silk fibroin as one of the materials for biomedical application.…”

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confidence: 99%

Cytocompatibility of silkworm cocoon layer extracts

Jo¹,

Kim²,

Lee³

et al. 2016

International Journal of Industrial Entomology

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Recently silk polymer produced by Bombyx mori silkworm has been considered as biological macromolecules. Silk polymer was extracted in PBS solution at 37 o C for 72 h or 72 o C for 24 h. The effect of EtOH treatment on the cocoon extraction was also examined. The extraction yield of cocoon was less than 1 wt% regardless of extraction conditions. UV spectroscopy showed that the experimental extracts have absorption bands at 280 nm. There is no cytotoxicity effect on the mouse fibroblast L929 cell. The phenotype of L929 cell was not changed under the experimental conditions. The proliferation behavior of L929 cell was not affected by the addition of cocoon extract. Therefore, cocoon extract might be cytocompatible and can be used as promising biomaterials. IntroductionA silkworm cocoon of Bombyx mori provides silk fiber for textile industries for more than 4,000 years. Recently, silk polymer has been revealed several advantages for biological materials and then applied various functional materials such as cosmetics, suture and artificial eardrum (Kundu et al., 2013;Ju et al., 2014;Vepari and Kaplan, 2007; Kim et al., 2010), and so on.In the view point of material, silk is a natural protein polymer composed of two proteins: one is a central protein called silk fibroin and another is gum-like protein called silk sericin. Silk fibroin is a natural fibrous protein with a semicrystalline structure and it consists of heavy chain (390 kDa), light chain (25 kDa) and glycoprotein. Each polypeptides linked by disulfide bond (Zhou et al., 2001).Especially, fibroin as the main component of silk protein has found diverse applications in the biomedical field, which has a strong tensile strength, biodegradability and biocompatibility (Horan et al., 2005;Meinel et al., 2005). Hence, many researchers select silk fibroin as one of the materials for biomedical application.Silk sericin is a protein polymer, which acts as an adhesive binder to maintain the structure of the fibers. Sericin is an albuminoid protein composed of serine (30%) and other amino acids (Teramoto and Miyazawa, 2005;Garel et al., 1997). Sericin was removed easily from Bombyx mori cocoon using a thermo or chemical process called degumming (Mo et al., 2009) Preparation of cocoon extractsEach cocoon was washed with tap water and then dried absolutely with room temperature in the dark. The cocoon was sliced into 5 mm ⅹ 5 mm pieces. Each cocoon slices were divided into two groups; one group was treated with absolute ethyl alcohol (EtOH) for 24 h at R.T. and another group was not treated EtOH. After treatment, cocoon was dried with R.T. for overnight. The extraction condition were followed; weigh 1 g of cocoon and add into 10 mL of 1X PBS buffer at 37 o C for 72 h and/or 72 o C for 24 h. Save the cocoon extracts and then filtered it with 0.22 um syringe filter (Sartorius Ltd., Epsom, UK) and protein concentration of all extracts was determined by bicinchronic acid (BCA) assay. Forty ug of each extracts used for cell cytotoxicity and proliferation assay. UV vis sp...

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Silk fibroin: Structural implications of a remarkable amino acid sequence

Cited by 650 publications

References 9 publications

Graphene Oxide/Polymer‐Based Biomaterials

Graphene Oxide/Polymer‐Based Biomaterials

Chemoenzymatic Synthesis of Polypeptides for Use as Functional and Structural Materials

Cytocompatibility of silkworm cocoon layer extracts

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