Honeybee silk: Recombinant protein production, assembly and fiber spinning

Weisman, Sarah; Haritos, Victoria S.; Church, Jeffrey S.; Huson, Mickey G.; Mudie, Stephen; Rodgers, Andrew J.W.; Dumsday, Geoff; Sutherland, Tara D.

doi:10.1016/j.biomaterials.2009.12.021

Cited by 75 publications

(106 citation statements)

References 15 publications

(30 reference statements)

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“…The underlying small genes (approximately 1 kbp) have been identified, and the respective cDNA was cloned into pET expression vectors to produce full-length proteins AmelF1-4 (A. mellifera fibroin 1-4) in E. coli Rosetta. Due to the small protein sizes, good yields of up to 2.5 g/l of ferment were obtained [49]. Interestingly, homologous sets of four silk encoding genes have been reported for other animals, e.g.…”

Section: Bee Silkmentioning

confidence: 99%

“…An equimolar mix of the four honey bee silk proteins AmelF1-4 was cast into a film and investigated concerning secondary structure content using FTIR [49]. Native honeybee silk (washed in chloroform to remove wax) contained approximately 65% of coiled-coil structure, and the film cast from the recombinant silk exhibited similar values.…”

Section: Examplesmentioning

confidence: 99%

“…In order to analyse the fibre-forming properties of recombinant honey bee silk, aqueous solutions of AmelF1-F4 were prepared and concentrated using polyethylene glycol (PEG) dialysis [49]. Solutions containing only one of the proteins started to precipitate at 2-4% (w/v), and no fibres could be drawn from these low concentrations.…”

Section: Examplesmentioning

confidence: 99%

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Applicability of biotechnologically produced insect silks

Herold

Scheibel

2017

Zeitschrift Für Naturforschung C

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Silks are structural proteins produced by arthropods. Besides the well-known cocoon silk, which is produced by larvae of the silk moth Bombyx mori to undergo metamorphosis inside their silken shelter (and which is also used for textile production by men since millennia), numerous further less known silk-producing animals exist. The ability to produce silk evolved multiple independent times during evolution, and the fact that silk was subject to convergent evolution gave rise to an abundant natural diversity of silk proteins. Silks are used in air, under water, or like honey bee silk in the hydrophobic, waxen environment of the bee hive. The good mechanical properties of insect silk fibres together with their non-toxic, biocompatible, and biodegradable nature renders these materials appealing for both technical and biomedical applications. Although nature provides a great diversity of material properties, the variation in quality inherent in materials from natural sources together with low availability (except from silkworm silk) impeded the development of applications of silks. To overcome these two drawbacks, in recent years, recombinant silks gained more and more interest, as the biotechnological production of silk proteins allows for a scalable production at constant quality. This review summarises recent developments in recombinant silk production as well as technical procedures to process recombinant silk proteins into fibres, films, and hydrogels.

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Section: Bee Silkmentioning

confidence: 99%

Section: Examplesmentioning

confidence: 99%

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Applicability of biotechnologically produced insect silks

Herold

Scheibel

2017

Zeitschrift Für Naturforschung C

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“…However, attempts to date make use of non-natural processing steps, such as solubilization in hexafluoroacetone [58] or detergent micelles [35,51,60], and solidification using methanol baths [35,60]. It is not clear what kind of liquid crystal phenomena, if any, occur during these types of material fabrication.…”

Section: Multiple Trajectories Through Liquidmentioning

confidence: 99%

“…300 nm for the TMV) and hence might be used to introduce structure at finer scales compared with virion mesogens. In addition, non-canonical silk proteins are easily engineered, express at high levels and are easily refolded into native-like conformations [28,35,60]. However, the greatest advantage of non-canonical silk proteins over alternative protein mesogens, such as virus particles, is that liquid crystalline processing into solid materials is their natural function.…”

Section: Multiple Trajectories Through Liquidmentioning

confidence: 99%

More than one way to spin a crystallite: multiple trajectories through liquid crystallinity to solid silk

2015

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Arthropods face several key challenges in processing concentrated feedstocks of proteins (silk dope) into solid, semi-crystalline silk fibres. Strikingly, independently evolved lineages of silk-producing organisms have converged on the use of liquid crystal intermediates (mesophases) to reduce the viscosity of silk dope and assist the formation of supramolecular structure. However, the exact nature of the liquid-crystal-forming-units (mesogens) in silk dope, and the relationship between liquid crystallinity, protein structure and silk processing is yet to be fully elucidated. In this review, we focus on emerging differences in this area between the canonical silks containing extended-bsheets made by silkworms and spiders, and 'non-canonical' silks made by other insect taxa in which the final crystallites are coiled-coils, collagen helices or cross-b-sheets. We compared the amino acid sequences and processing of natural, regenerated and recombinant silk proteins, finding that canonical and non-canonical silk proteins show marked differences in length, architecture, amino acid content and protein folding. Canonical silk proteins are long, flexible in solution and amphipathic; these features allow them both to form large, micelle-like mesogens in solution, and to transition to a crystallite-containing form due to mechanical deformation near the liquidsolid transition. By contrast, non-canonical silk proteins are short and have rod or lath-like structures that are well suited to act both as mesogens and as crystallites without a major intervening phase transition. Given many non-canonical silk proteins can be produced at high yield in E. coli, and that mesophase formation is a versatile way to direct numerous kinds of supramolecular structure, further elucidation of the natural processing of non-canonical silk proteins may to lead to new developments in the production of advanced protein materials.

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Silk‐Based Biomaterials in Biomedical Textiles and Fiber‐Based Implants

Chen

et al. 2015

Adv Healthcare Materials

144

103

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Biomedical textiles and fiber-based implants (BTFIs) have been in routine clinical use to facilitate healing for nearly five decades. Amongst the variety of biomaterials used, silk-based biomaterials (SBBs) have been widely used clinically viz. sutures for centuries and are being increasingly recognized as a prospective material for biomedical textiles. The ease of processing, controllable degradability, remarkable mechanical properties and biocompatibility have prompted the use of SBBs for various BTFIs for extracorporeal implants, soft tissue repair, healthcare/hygiene products and related needs. The present review focuses on BTFIs from the perspective of types and physical and biological properties, and this discussion is followed with an examination of the advantages and limitations of BTFIs from SBBs. The review covers progress in surface coatings, physical and chemical modifications of SBBs for BTFIs and identifies future needs and opportunities for the further development for BTFIs using SBBs.

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Honeybee silk: Recombinant protein production, assembly and fiber spinning

Cited by 75 publications

References 15 publications

Applicability of biotechnologically produced insect silks

Applicability of biotechnologically produced insect silks

More than one way to spin a crystallite: multiple trajectories through liquid crystallinity to solid silk

Silk‐Based Biomaterials in Biomedical Textiles and Fiber‐Based Implants

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