Processing and modification of films made from recombinant spider silk proteins

Huemmerich, Daniel; Slotta, Ute; Scheibel, Thomas

doi:10.1007/s00339-005-3428-5

Cited by 142 publications

(150 citation statements)

References 17 publications

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“…Strikingly, out of the mixture fibers assembled similar to those of eADF3 alone ( . To visualize the potential incorporation of eADF4, we partially labeled (10% wt/wt) eADF4 with the f luorescent dye FITC (9). Fluorescent micrographs revealed homogenously distributed eADF4 in the assembled fiber (Fig.…”

Section: Resultsmentioning

confidence: 99%

“…S1 and Materials and Methods]. Under distinct solvent conditions these engineered silk proteins controllably assemble into different morphologies, such as nanofibrils (6), hydrogels (7), films (9,10), and microcapsules (11). Further, conditions for a liquidliquid phase separation have been identified, leading to large colloidal assemblies that likely reflect a prerequisite for silk fiber formation (12).…”

mentioning

confidence: 99%

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Assembly mechanism of recombinant spider silk proteins

Rammensee¹,

Slotta

Scheibel

et al. 2008

Proc. Natl. Acad. Sci. U.S.A.

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356

377

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Spider silk threads are formed by the irreversible aggregation of silk proteins in a spinning duct with dimensions of only a few micrometers. Here, we present a microfluidic device in which engineered and recombinantly produced spider dragline silk proteins eADF3 (engineered Araneus diadematus fibroin) and eADF4 are assembled into fibers. Our approach allows the direct observation and identification of the essential parameters of dragline silk assembly. Changes in ionic conditions and pH result in aggregation of the two proteins. Assembly of eADF3 fibers was induced only in the presence of an elongational flow component. Strikingly, eADF4 formed fibers only in combination with eADF3. On the basis of these results, we propose a model for dragline silk aggregation and early steps of fiber assembly in the microscopic regime.colloids ͉ microfluidics ͉ protein materials ͉ rheology

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Section: Resultsmentioning

confidence: 99%

mentioning

confidence: 99%

Assembly mechanism of recombinant spider silk proteins

Rammensee¹,

Slotta

Scheibel

et al. 2008

Proc. Natl. Acad. Sci. U.S.A.

Self Cite

356

377

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show abstract

“…Post treatment of the films with organic solvents like methanol resulted in further rearrangements of protein structure, increasing the β-sheet content dramatically. [71][72][73] Figure 5. Possible shapes of spider silk.…”

Section: Mimicking Naturementioning

confidence: 99%

The elaborate structure of spider silk

Römer

Scheibel

2008

Prion

314

179

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“…Silk III assembles at an air (or oil)/water interface [8], but only silk I and silk II are of interest in this work. Water-soluble silk I can be converted to insoluble silk II by exposure to methanol, as reported by Huemmerich et al [9]. The asymmetrical b-sheet structures of Silk II consist of hydrogen side chains from glycine on one side and methyl side chains from alanine on the other side.…”

Section: Introductionmentioning

confidence: 73%

Biocompatible silk fibroin scaffold prepared by reactive inkjet printing

et al. 2016

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It has recently been shown that regenerated silk fibroin (RSF) aqueous solution can be printed using an inkjet printer. In this communication, we demonstrate an alternative reactive inkjet printing method that provides control over RSF crystallinity through b-sheet concentration. A biocompatible film has successfully been produced through the alternate printing of RSF aqueous solution and methanol using reactive inkjet printing. Control over the formation of the bsheet structure was achieved by printing different ratios of RSF to methanol and was confirmed using Fourier Transform Infra Red spectroscopy. The biocompatibility of the printed silk scaffold was demonstrated by the growth of fibroblast cells upon its surface.Silk is a versatile, natural material favoured for its mechanical strength, excellent biocompatibility, adaptable biodegradability [1, 2], easy processing [3] and flexible structural modification [4]. Silk has a long history of use [5]; recently, regenerated silk fibroin (RSF) has been used as a building block for the fabrication of biomedical devices [3]. RSF structures are commonly produced with a casting method; however, additive manufacture applications offer a greater control over RSF film surfaces which can be advantageous for controlling cell growth. Current additive manufacture applications are mainly focused on producing individual silk fibres such as electrohydrodynamic printing [6] and electrospinning [7]. Different silk polymorphs, silk I, silk II and silk III, have been observed. Silk I, which is the water-soluble state seen prior to crystallisation, is composed of ahelix and amorphous chains. Silk II contains an extended b-sheet structure and appears after spinning [3]. Silk III assembles at an air (or oil)/water interface [8], but only silk I and silk II are of interest in this work. Water-soluble silk I can be converted to insoluble silk II by exposure to methanol, as reported by Huemmerich et al. [9]. The asymmetrical b-sheet structures of Silk II consist of hydrogen side chains from glycine on one side and methyl side chains from alanine on the other side. The methyl groups interact with hydrogen groups of opposing b-sheets to form

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Processing and modification of films made from recombinant spider silk proteins

Cited by 142 publications

References 17 publications

Assembly mechanism of recombinant spider silk proteins

Assembly mechanism of recombinant spider silk proteins

The elaborate structure of spider silk

Biocompatible silk fibroin scaffold prepared by reactive inkjet printing

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