The role of terminal domains during storage and assembly of spider silk proteins

  title={The role of terminal domains during storage and assembly of spider silk proteins},
  author={Lukas Eisoldt and Christopher Thamm and Thomas R Scheibel},
Fibrous proteins in nature fulfill a wide variety of functions in different structures ranging from cellular scaffolds to very resilient structures like tendons and even extra‐corporal fibers such as silks in spider webs or silkworm cocoons. Despite their different origins and sequence varieties many of these fibrous proteins share a common building principle: they consist of a large repetitive core domain flanked by relatively small non‐repetitive terminal domains. Amongst protein fibers… 
Uncovering the structure-function relationship in spider silk
All spiders produce protein-based biopolymer fibres that we call silk. The most studied of these silks is spider dragline silk, which is very tough and relatively abundant compared with other types
The N-terminal domains of spider silk proteins assemble ultrafast and protected from charge screening.
This work engineers a fluorescence switch into the isolated N-terminal domain from spidroin 1 of the major ampullate gland of the nursery web spider E. australis that monitors dimerization, and mutates each of the protonatable residue side chains and probes their contributions.
To spin or not to spin: spider silk fibers and more
The different approaches of biotechnological production and the advances in material processing toward various applications will be reviewed.
Two-step self-assembly of a spider silk molecular clamp
A previously unknown three-state mechanism of folding and an expanded structure of a spider silk protein that may contribute to elasticity of spider silk are reported.
Silk Spinning in Silkworms and Spiders
It is suggested that factors that need to be optimized for successful production of artificial silk proteins capable of forming tough fibers include protein solubility, pH sensitivity, and preservation of natively folded proteins throughout the purification and initial spinning processes.
From silk spinning in insects and spiders to advanced silk fibroin drug delivery systems.
  • Vera Werner, L. Meinel
  • Materials Science
    European journal of pharmaceutics and biopharmaceutics : official journal of Arbeitsgemeinschaft fur Pharmazeutische Verfahrenstechnik e.V
  • 2015
Methionine in a protein hydrophobic core drives tight interactions required for assembly of spider silk
The authors show that the tight binding of a spider silk protein domain relies on the amino acid methionine, which is abundant in the domain core where it facilitates dynamic shape adaption of the binding interface.
Conservation of folding and association within a family of spidroin N-terminal domains
Results showed that energetics and kinetics of NTD self-assembly are highly conserved across spider species despite the different silk mechanical properties and web geometries they produce.
Silk nanofibril self-assembly versus electrospinning.
Self-assembly of silk proteins into hierarchically organized structures such as supramolecular nanofibrils and fabricated materials based thereon is introduced as an alternative to self-assembly and electrospinning a technique to produce nanofibers and nan ofibrous mats is presented.
More than just fibers: an aqueous method for the production of innovative recombinant spider silk protein materials.
A method to rapidly dissolve rSSps in water in lieu of traditional organic solvents and accomplish nearly 100% solvation and recovery of the protein, the only method that is cost-effective and scalable for mass production.


A conserved spider silk domain acts as a molecular switch that controls fibre assembly
Evidence is provided that the structural state of this domain is essential for controlled switching between the storage and assembly forms of silk proteins and has a role in the alignment of secondary structural features formed by the repetitive elements in the backbone of spider silk proteins, which is known to be important for the mechanical properties of the fibre.
Self-assembly of spider silk proteins is controlled by a pH-sensitive relay
It is discovered that incorporation of the amino-terminal domain of major ampullate spidroin 1 from the dragline of the nursery web spider Euprosthenops australis into mini-spidroins enables immediate, charge-dependent self-assembly at pH values around 6.3, but delays aggregation above pH 7.
Macroscopic fibers self-assembled from recombinant miniature spider silk proteins.
It is here demonstrated that a miniature spidroin from a protein in dragline silk of Euprosthenops australis can be produced in a soluble form in Escherichia coli when fused to a highly soluble protein partner.
Mechanism of silk processing in insects and spiders
Emulsion formation and micellar structures from aqueous solutions of reconstituted silkworm silk fibroin are identified as a first step in the process to control water and protein–protein interactions and mimics the behaviour of similar native silk proteins in vivo.
Assembly mechanism of recombinant spider silk proteins
A microfluidic device in which engineered and recombinantly produced spider dragline silk proteins eADF3 (engineered Araneus diadematus fibroin) and eadF4 are assembled into fibers is presented and a model for dragline Silk aggregation and early steps of fiber assembly in the microscopic regime is proposed.
Silk Properties Determined by Gland-Specific Expression of a Spider Fibroin Gene Family
A gene family from the spider Araneus diadematus was found to encode silk-forming proteins (fibroins) with different proportions of amorphous glycine-rich domains and crystal domains built from poly(alanine) and poly(glycine-alanine), which allows for a range of mechanical properties according to the crystal-forming potential of the constituent fibroins.
Primary structure elements of spider dragline silks and their contribution to protein solubility.
Comparing secondary structure, solubility, and aggregation properties of the synthesized proteins revealed that single primary structure elements have diverse influences on protein characteristics, and engineered proteins comprising the carboxyl-terminal nonrepetitive regions of ADF-3 orADF-4 might play an important role in initiating assembly of spider silk proteins.
Spider silk: from soluble protein to extraordinary fiber.
This work presents natural and artificial silk production processes, from gene transcription to silk protein processing and finally fiber assembly, which will enable applications of these fascinating protein-based materials in technical and medical sciences.
Differential polymerization of the two main protein components of dragline silk during fibre spinning
The findings suggest that the role of spidroin 2 in the spinning process could be to facilitate the formation of fibrils and contribute directly to the elasticity of the silk.