Temperature dependent structure of spider silk by X-ray diffraction

Glišović, Anja; Salditt, Tim

doi:10.1007/s00339-006-3849-9

Cited by 42 publications

(28 citation statements)

References 17 publications

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“…Reflection profiles were radially or azimuthally integrated with a region of 180°and fitted by Lorenz profiles. 16 The position for amorphous region of the samples in the intensity profile was evaluated to be at the d-spacing of 4.1 Å by using an amorphous RSF film cast from RSF aqueous solution. The crystallinity of the fiber was then determined by peak separation analysis.…”

Section: Characterizationmentioning

confidence: 99%

A simple process for dry spinning of regenerated silk fibroin aqueous solution

et al. 2013

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The conventional process for preparing dry spinnable regenerated silk fibroin (RSF) aqueous solution needs not only an addition of Ca 21 but also an adjustment of pH value. In this work, an RSF dry spinning dope was prepared by using a simplified method with solely adding Ca 21 . Compared with the conventional RSF solution, the simply prepared aqueous solution showed similar content of b-sheet conformation and diameter of RSF aggregates but lower viscosity. Furthermore, the posttreated RSF fiber dry-spun from this simply prepared solution showed higher crystallinity and crystalline orientation, smaller crystallite size, and better mechanical properties. It could be concluded that Ca 21 played a much more important role than pH value in improving the structures and properties of RSF spinning solution and fibers. Therefore, the step of adjusting pH value could be excluded in the process of preparing high performance RSF fibers.

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Section: Characterizationmentioning

confidence: 99%

A simple process for dry spinning of regenerated silk fibroin aqueous solution

et al. 2013

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“…Nuclear magnetic resonance and X-ray diffraction studies revealed a high content of crystalline domains consisting of poly-A antiparallel β-sheets, packed into an orthorhombic unit cell with dimensions of at least 2×5× 7 nm (Warwicker 1960;Glisovic and Salditt 2007). These domains provide the tensile strength of silk fiber, while the Gly-rich matrix is responsible for the elasticity (Simmons et al 1994;Parkhe et al 1997;van Beek et al 2002).…”

Section: Introductionmentioning

confidence: 98%

A Novel Model System for Design of Biomaterials Based on Recombinant Analogs of Spider Silk Proteins

Богуш

Sokolova

Давыдова

et al. 2008

J Neuroimmune Pharmacol

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Spider dragline silk possesses impressive mechanical and biochemical properties. It is synthesized by a couple of major ampullate glands in spiders and comprises of two major structural proteins--spidroins 1 and 2. The relationship between structure and mechanical properties of spider silk is not well understood. Here, we modeled the complete process of the spider silk assembly using two new recombinant analogs of spidroins 1 and 2. The artificial genes sequence of the hydrophobic core regions of spidroin 1 and 2 have been designed using computer analysis of existing databases and mathematical modeling. Both proteins were expressed in Pichia pastoris and purified using a cation exchange chromatography. Despite the absence of hydrophilic N- and C-termini, both purified proteins spontaneously formed the nanofibrils and round micelles of about 1 microm in aqueous solutions. The electron microscopy study has revealed the helical structure of a nanofibril with a repeating motif of 40 nm. Using the electrospinning, the thin films with an antiparallel beta-sheet structure were produced. In summary, we were able to obtain artificial structures with characteristics that are perspective for further biomedical applications, such as producing three-dimensional matrices for tissue engineering and drug delivery.

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“…[34,35] The broadening observed in this work, however, could mainly be attributed to the crystallite size because spider silk is known to have a high thermal stability. [36] In addition, the peak intensity ratio, that is, @I [I B,max /I A,max ] also revealed variations. Initially, the intensity ratio of SS/N, that is, @I SS/N = [I B,max /I A,max ] SS/N , was around 2.9.…”

Section: Changes In Protein Structures By Ald and Cvdmentioning

confidence: 95%

“…In contrast, the @I SS/CVD remained nearly unchanged ( % 2.9). Consequently, the variation of @I should be caused by the change of the total number of b-sheet crystallites in the silk protein or by a slight change of the amino acid composition of the b-sheet crystallite [36] after ALD. In the case of the collagen membrane, b sheets are not present.…”

Section: Changes In Protein Structures By Ald and Cvdmentioning

confidence: 98%

Metal Infiltration into Biomaterials by ALD and CVD: A Comparative Study

2011

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Atomic layer deposition (ALD) is a subset of chemical vapor deposition (CVD) and both use very similar chemistry. Recently, it has been reported that ALD has the potential to realize a new design paradigm of bioinorganic materials through metal infiltration, which in nature has been employed as a hardening strategy for many tissues in diverse biological organisms. Herein, using a spider dragline silk and a collagen membrane as targets, we have performed a comparative study to elucidate the difference of the metal infiltration effect by ALD and CVD. From the comparison of mechanical properties, concentration of the infiltrated metal, and structural changes induced by the infiltrated metal, it has been proven that the metal can effectively infiltrate biomaterials by ALD and the infiltrated metal leads to highly improved mechanical properties accompanied by substantial changes in the protein structures, whereas CVD is less effective.

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Temperature dependent structure of spider silk by X-ray diffraction

Cited by 42 publications

References 17 publications

A simple process for dry spinning of regenerated silk fibroin aqueous solution

A simple process for dry spinning of regenerated silk fibroin aqueous solution

A Novel Model System for Design of Biomaterials Based on Recombinant Analogs of Spider Silk Proteins

Metal Infiltration into Biomaterials by ALD and CVD: A Comparative Study

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