Spider silk proteins: recent advances in recombinant production, structure–function relationships and biomedical applications

Rising, Anna; Widhe, Mona; Johansson, Jan; Hedhammar, My

doi:10.1007/s00018-010-0462-z

Cited by 177 publications

(155 citation statements)

References 132 publications

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“…The possibility of tracing varied molecular composition effects on macroscale behavior is realized experimentally through recombinant silk production mimicking the spider spinning process, outlining a powerful multiscale approach that incorporates experiment and simulation. 39 Amino acid sequence Primary protein structure (Å ) The primary protein structure is composed of a sequence of amino acid residues which define the folding of subsequent hierarchical levels. In silk, poly-alanine regions are responsible for stiff cross-linking domains while glycine-rich regions define structures within amorphous domains Basic building block that dictates secondary protein structure.…”

Section: Resultsmentioning

confidence: 99%

“…18,20,23 Recent work in genetic engineering and peptide synthesis has been successful in sequencing silk genes and using this information to generate recombinant engineered versions of the natural protein. 38,39 Beta-sheet nanocrystals Secondary protein structure (nm) The secondary protein structure defines local conformations, such as alpha-helices and beta-turns. Beta-sheet crystals in silk have a critical size of 2 nm to 4 nm, exhibiting exceptional strength due to cooperative hydrogen bonding between the sheets.…”

Section: Resultsmentioning

confidence: 99%

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A Materiomics Approach to Spider Silk: Protein Molecules to Webs

Tarakanova

Buehler

2012

JOM

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The exceptional mechanical properties of hierarchical self-assembling silk biopolymers have been extensively studied experimentally and in computational investigations. A series of recent studies has been conducted to examine structure-function relationships across different length scales in silk, ranging from atomistic models of protein constituents to the spider web architecture. Silk is an exemplary natural material because its superior properties stem intrinsically from the synergistic cooperativity of hierarchically organized components, rather than from the superior properties of the building blocks themselves. It is composed of beta-sheet nanocrystals interspersed within less orderly amorphous domains, where the underlying molecular structure is dominated by weak hydrogen bonding. Protein chains are organized into fibrils, which pack together to form threads of a spider web. In this article we survey multiscale studies spanning length scales from angstroms to centimeters, from the amino acid sequence defining silk components to an atomistically derived spider web model, with the aim to bridge varying levels of hierarchy to elucidate the mechanisms by which structure at each composite level contributes to organization and material phenomena at subsequent levels. The work demonstrates that the web is a highly adapted system where both material and hierarchical structure across all length scales is critical for its functional properties.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

A Materiomics Approach to Spider Silk: Protein Molecules to Webs

Tarakanova

Buehler

2012

JOM

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“…It is thus generally difficult to maintain the spidroins in solution, especially at high concentration. 215 To mimic natural conditions, high concentrations may be required although it has been found that 15% is an optimal concentration for synthetic spinning. It seems in any case difficult to exceed 20-25 % w/w and, for the moment, difficult to reach the native concentration found in the gland ampulla and to keep the solution stable.…”

Section: Wet Spinningmentioning

confidence: 99%

Spider silk as a blueprint for greener materials: a review

Lefèvre

Auger

2016

International Materials Reviews

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Spider silk exhibits remarkable properties, especially its well-known tensile performances. They rely on a complex nanostructured hierarchical organization that researches progressively elucidate. Spider silk encompasses a vast range of fibers that exhibit diverse and captivating physical and biological characteristics. The full understanding of the relation between structure and properties may lead in the future to the design of a variety of high-performance, tailored materials and devices. Reknown for being produced in mild and begnin conditions, this outstanding biological material constitutes one the more representative example of biomimetism. In addition, silk's structure is produced with limited means, i.e. low energy and relatively simple renewable constituents (silk proteins). Then, if successfully controlled and adequately transposed in biomaterials, some properties of natural silk could lead to innovative green materials that may contribute to reduce the ecological footprint of societies. In fact, striking recent advanced applications made with B. mori silk suggest that spider silk-based materials may lead to advanced resistant and functional materials, then becoming among the most promising subject of study in material science. However, several challenges have to be overcome, especially our ability to produce native-like silk, to control biomaterials' structure and properties, and to minimize their ecological footprint. This paper reviews the characteristics of spider silk that make it so attractive and that may (or may not) contribute to reduce ecological footprint of materials and the challenges in producing innovative spider silk-based materials. First, from a biomimetic perspective, the structure and models that explain the tensile resistance of natural silk are presented, followed by the state of knowledge regarding natural silk spinning process and synthetic production methods. Biocompatibility (biosafety and biofunctionality) as well as biodegradability issues are then addressed. Finally, examples of applications are reviewed. Features that may lead to the design of green materials are emphasized throughout.

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“…For details see recent reviews on human collagens, 1 mussel pre-collagens, 2,3 silkworm silk, 4,5 and spider silk. [6][7][8][9] Here, we highlight some similarities concerning assembly of the proteins into fibers. All four protein classes exhibit a highly repetitive core region with specific amino acid motifs repeated up to several hundred times.…”

Section: Introductionmentioning

confidence: 99%

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

2011

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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, spider dragline silk shows prominent mechanical properties that exceed those of man‐made fibers like Kevlar. Spider silk fibers assemble in a spinning process allowing the transformation from an aqueous solution into a solid fiber within milliseconds. Here, we highlight the role of the non‐repetitive terminal domains of spider dragline silk proteins during storage in the gland and initiation of the fiber assembly process. © 2011 Wiley Periodicals, Inc. Biopolymers 97: 355–361, 2012.

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Spider silk proteins: recent advances in recombinant production, structure–function relationships and biomedical applications

Cited by 177 publications

References 132 publications

A Materiomics Approach to Spider Silk: Protein Molecules to Webs

A Materiomics Approach to Spider Silk: Protein Molecules to Webs

Spider silk as a blueprint for greener materials: a review

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

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