Biomimetic Fibers Made of Recombinant Spidroins with the Same Toughness as Natural Spider Silk

Heidebrecht, Aniela; Eisoldt, Lukas; Diehl, Johannes; Schmidt, Andreas; Geffers, Martha; Lang, Gregor; Scheibel, Thomas

doi:10.1002/adma.201404234

Cited by 226 publications

(330 citation statements)

References 49 publications

Supporting

Mentioning

320

Contrasting

Unclassified

Order By: Relevance

“…1,2 While first attempts to synthesize silk fibers have been successful, and industry-scale production of recombinant silk is possible, the mechanical properties of the spun fibers either do not currently compare with natural fibers or the assembly is performed under non-ambient conditions. 3,4 Furthermore, many synthesized fibers contain a substantial amount of regenerated silk, i.e. the spinning dope originates from natural spider silk.…”

Section: Introductionmentioning

confidence: 99%

“…the spinning dope originates from natural spider silk. 4 Using genetically engineered sequences presents a way to reduce limitations on fiber supply from spiders, but yields weaker and more brittle fibers. 5 The inferior quality of the engineered fibers mainly arises from the selection of assembly process parameters in industrial spinning devices, different rheological behavior and molecular weights of the material.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Secondary Structure Transition and Critical Stress for a Model of Spider Silk Assembly

2016

View full text Add to dashboard Cite

Spiders spin their silk from an aqueous solution to a solid fiber in ambient conditions. However, to date the assembly mechanism in the spider silk gland has not been satisfactorily explained. In this paper, we use molecular dynamics simulations to model N. clavipes MaSp1 dragline silk formation under shear flow and determine the secondary structure transitions leading to the experimentally observed fiber structures. While no experiments are performed on the silk fiber itself, insights from this polypeptide model can be transferred to the fiber scale. The novelty of this study lies in the calculation of the shear stress (300-700 MPa) required for fiber formation and identification of the amino acid residues involved in the transition. This is the first time that the shear stress has been quantified in connection with a secondary structure transition. By study of molecules containing varying numbers of contiguous MaSp1 repeats we identified the smallest molecule size that gives rise to a 'silk-like' structure contains six poly-alanine repeats.Through a probability analysis of the secondary structure we identify specific amino acids that transition from α-helix to β-sheet. In addition to portions of the poly-alanine section these amino acids include glycine, leucine and glutamine. Stability of β-sheet structures appears to arise from a close proximity in space of helices in the initial spidroin state. Our results are in agreement with the forces exerted by spiders in the silking process and the experimentally determined global secondary structure of spidroin and pulled MaSp1 silk. Our study emphasizes the role of shear in the assembly process of silk and can guide the design of microfluidic devices that attempt to mimic the natural spinning process and predict molecular requirements for the next generation of silk-based functional materials.

show abstract

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Secondary Structure Transition and Critical Stress for a Model of Spider Silk Assembly

2016

View full text Add to dashboard Cite

show abstract

“…When one compare the mechanical data F 5 of molecular weight 47kD with the results obtained by Heidebrecht et al [22], one can find relatively good output because the present technique uses economic and nontoxic ASs.…”

Section: Mechanical Properties Of Recombinant-spider Dragline Silksmentioning

confidence: 78%

“…Heidebrecht et al [22] have found that starting with protein with molecular weight 120kD produced excellent flexible RSDSs having cutoff strength of 383 MPa with corresponding strain of 600% [22]. When one compare the mechanical data F 5 of molecular weight 47kD with the results obtained by Heidebrecht et al [22], one can find relatively good output because the present technique uses economic and nontoxic ASs.…”

Section: Mechanical Properties Of Recombinant-spider Dragline Silksmentioning

confidence: 85%

See 1 more Smart Citation

Preparation and Characterization of Artificial Spider Silk Produced through Microchannel Techniques

Abdalla¹,

Obaid²,

Al-Marzouki³

et al. 2017

J Material Sci Eng

View full text Add to dashboard Cite

Spider silk (SS) is naturally tough; however, it turns soft when wet by water. Spiders produce high-quality silk threads by adjusting the molecular assemblage of SS-proteins and the arrangements structure of threads and recombinant spider dragline silk (RSDS). The general wet spinning techniques for producing recombinant spidroins results in uncorrected explanation to the natural spinning technique. In this study, we use tailored-SS with relative low molecular weight of 47 kD to produce a water-soluble RSDS protein. We built a microfluidic ship and used it to spun SS using aqueous solutions-micro-technique (wet spinning). This was done in order to mimic the spider-spinning processes using a steady post-spin drawing process. We succeeded to produce assemblies of spidroins with fibril structure. Then, compact constituting of micro-threads followed these wet spinning processes. Wet spinning was followed by improving the orientation, crystalline structure, and fibril melting of the hierarchical structure. The initial mechanical characterization (tensile strength) of the RSDSs attained about 510 MPa with respective extension 44%.

show abstract

Materials Biomimicked From Natural Ones

Santulli

2023

Biomimicry Materials and Applications

View full text Add to dashboard Cite

Biomimetic Fibers Made of Recombinant Spidroins with the Same Toughness as Natural Spider Silk

Cited by 226 publications

References 49 publications

Secondary Structure Transition and Critical Stress for a Model of Spider Silk Assembly

Secondary Structure Transition and Critical Stress for a Model of Spider Silk Assembly

Preparation and Characterization of Artificial Spider Silk Produced through Microchannel Techniques

Materials Biomimicked From Natural Ones

Contact Info

Product

Resources

About