Interfacial rheological properties of recombinant spider-silk proteins

Vézy, Cyrille; Hermanson, Kevin D.; Scheibel, Thomas; Bausch, Andreas R.

doi:10.1116/1.3174930

Cited by 14 publications

(7 citation statements)

References 23 publications

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“…It is noteworthy that a different behavior was reported for the engineered spider silk protein C 16 in the study published by Vézy et al 28 At corresponding mass concentrations, the elastic modulus of C 16 at the water-oil interface (polydimethylsiloxane oil) had stagnated after approximately 70 min. C 16 (48 kDa) is constructed from 16 repetitions of a consensus sequence of the repetitive part from the spider Araneus diadematus, whereas the sequence of 4Rep (12 kDa) is derived directly from the native sequence from the spider E. australis.…”

Section: Rheology and Qcm-d Measurements Show That 4rep Proteins Readmentioning

confidence: 79%

“…27 The recombinant spider silk protein C 16 with 16 repeats of a consensus unit from the dragline silk protein ADF-4 has also been studied with interfacial shear rheology at the water-oil interface. 28 Herein we have investigated the interfacial behavior of the parts of an even smaller recombinant spider silk protein, 4RepCT, derived from MaSp1 of Euprosthenops australis, which spontaneously form silk-like fibers at the liquid-air interface. 26,29 4RepCT consists of four repetitions of alternated poly-alanine and glycine rich regions (4Rep) followed by a globular C-terminal domain (CT), which dimerizes via a disulfide bridge.…”

Section: Introductionmentioning

confidence: 99%

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Interfacial Behavior of Recombinant Spider Silk Protein Parts Reveals Cues on the Silk Assembly Mechanism

et al. 2018

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The mechanism of silk assembly, and thus the cues for the extraordinary properties of silk, can be explored by studying the simplest protein parts needed for the formation of silk-like materials. The recombinant spider silk protein 4RepCT, consisting of four repeats of polyalanine and glycine-rich segments (4Rep) and a globular C-terminal domain (CT), has previously been shown to assemble into silk-like fibers at the liquid-air interface. Herein, we study the interfacial behavior of the two parts of 4RepCT, revealing new details on how each protein part is crucial for the silk assembly. Interfacial rheology and quartz crystal microbalance with dissipation show that 4Rep interacts readily at the interfaces. However, organized nanofibrillar structures are formed only when 4Rep is fused to CT. A strong interplay between the parts to direct the assembly is demonstrated. The presence of either a liquid-air or a liquid-solid interface had a surprisingly similar influence on the assembly.

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Section: Rheology and Qcm-d Measurements Show That 4rep Proteins Readmentioning

confidence: 79%

Section: Introductionmentioning

confidence: 99%

Interfacial Behavior of Recombinant Spider Silk Protein Parts Reveals Cues on the Silk Assembly Mechanism

et al. 2018

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“…During the passage of the spinning dope from the lumen through the spinning duct to the spigot (the point at which the fiber exits the animal), the dope is exposed to shear forces which are known to encourage aggregation in a variety of globular and fibrillar proteins (Bekard and Dunstan, 2009, Cromwell et al, 2006, Hamilton-Brown et al, 2008, Hill et al, 2006, Vezy et al, 2009, Yamaura et al, 1982and Yamaura et al, 1985; we were therefore keen to find out if shear forces have an effect upon the aggregation of our recombinantly produced MA silk-like proteins in vitro.…”

Section: The Effect Of Shear On Protein Aggregationmentioning

confidence: 99%

The role of salt and shear on the storage and assembly of spider silk proteins

Eisoldt

Hardy

Heim

et al. 2010

Journal of Structural Biology

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Major ampullate silk fibers of orb web-weaving spiders have impressive mechanical properties due to the fact that the underlying proteins partially fold into helical/amorphous structures, yielding relatively elastic matrices that are toughened by anisotropic nanoparticulate inclusions (formed from stacks of β-sheets of the same proteins). In vivo the transition from soluble protein to solid fibers involves a combination of chemical and mechanical stimuli (such as ion exchange, extraction of water and shear forces). Here we elucidate the effects of such stimuli on the in vitro aggregation of engineered and recombinantly produced major ampullate silk-like proteins (focusing on structurefunction relationships with respect to their primary structures), and discuss their relevance to the storage and assembly of spider silk proteins in vivo.

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“…No doubt there are a number of reasons for this but some of them may be as follows. Firstly, there has been increased recognition that interfacial rheology may make an important contribution to various biological processes, such as alveoli function in the lungs [4 • ], various digestive and adsorption processes [5 • ,6], fibre formation [7] and membrane function [8]. Secondly, a number of new experimental techniques for measuring interfacial rheology have been developed that cover a wide range of temporal and spatial regimes.…”

Section: Introductionmentioning

confidence: 99%