Composition and Hierarchical Organisation of a Spider Silk

Sponner, Alexander; Vater, W; Monajembashi, Shamci; Unger, Eberhard; Grosse, Frank; Weißhart, Klaus

doi:10.1371/journal.pone.0000998

Cited by 185 publications

(256 citation statements)

References 48 publications

(94 reference statements)

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“…[22][23][24] Extreme Poisson's ratios (1.29 and À0.48 for axial and radial deformation of N. clavipes silk) recently reported for major ampullate silks 25 reinforce the notion that spider silk should be viewed as a complex hierarchical structure rather than a continuum material.…”

Section: Properties Of Spider Silkmentioning

confidence: 62%

With great structure comes great functionality: Understanding and emulating spider silk

et al. 2014

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The overarching aim of biomimetic approaches to materials synthesis is to mimic simultaneously the structure and function of a natural material, in such a way that these functional properties can be systematically tailored and optimized. In the case of synthetic spider silk fibers, to date functionalities have largely focused on mechanical properties. A rapidly expanding body of literature documents this work, building on the emerging knowledge of structure-function relationships in native spider silks, and the spinning processes used to create them. Here, we describe some of the benchmark achievements reported until now, with a focus on the last five years. Progress in protein synthesis, notably the expression on full-size spidroins, has driven substantial improvements in synthetic spider silk performance. Spinning technology, however, lags behind and is a major limiting factor in biomimetic production. We also discuss applications for synthetic silk that primarily capitalize on its nonmechanical attributes, and that exploit the remarkable range of structures that can be formed from a synthetic silk feedstock.

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Section: Properties Of Spider Silkmentioning

confidence: 62%

With great structure comes great functionality: Understanding and emulating spider silk

et al. 2014

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“…Previous investigations have indicated the fibrillar nature of silk, and have proposed the so-called skin-core structural model-a bundle of silk fibrils encapsulated by an outer layer [39,[43][44][45][46], depicted in figure 1. The skin is thin with no discernible distinct features [44], even at failure [39], suggesting the core dominates mechanical properties.…”

Section: Introductionmentioning

confidence: 99%

“…The skin is thin with no discernible distinct features [44], even at failure [39], suggesting the core dominates mechanical properties. The skin-shown to contain an abundance of glycoproteins [43,46]-may play a key in the adhesion properties of silk [47,48]. That being said, few studies have explicitly considered the contribution of interfibril interactions to the response of a thread.…”

Section: Introductionmentioning

confidence: 99%

Increasing silk fibre strength through heterogeneity of bundled fibrils

Cranford

2013

J. R. Soc. Interface.

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Can naturally arising disorder in biological materials be beneficial? Materials scientists are continuously attempting to replicate the exemplary performance of materials such as spider silk, with detailed techniques and assembly procedures. At the same time, a spider does not precisely machine silk-imaging indicates that its fibrils are heterogeneous and irregular in cross section. While past investigations either focused on the building material (e.g. the molecular scale protein sequence and behaviour) or on the ultimate structural component (e.g. silk threads and spider webs), the bundled structure of fibrils that compose spider threads has been frequently overlooked. Herein, I exploit a molecular dynamics-based coarse-grain model to construct a fully three-dimensional fibril bundle, with a length on the order of micrometres. I probe the mechanical behaviour of bundled silk fibrils with variable density of heterogenic protrusions or globules, ranging from ideally homogeneous to a saturated distribution. Subject to stretching, the model indicates that cooperativity is enhanced by contact through low-force deformation and shear 'locking' between globules, increasing shear stress transfer by up to 200 per cent. In effect, introduction of a random and disordered structure can serve to improve mechanical performance. Moreover, addition of globules allows a tuning of free volume, and thus the wettability of silk (with implications for supercontraction). These findings support the ability of silk to maintain near-molecular-level strength at the scale of silk threads, and the mechanism could be easily adopted as a strategy for synthetic fibres.

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“…The mechanical properties of spider silk originate from the core of the fibre, which is protected by a series of 'skin' layers 1 (Figure 1). The outer core (≈15% of the radius) is thought to consist mainly of the highly ordered protein Spidroin I, with the inner core (≈80% of the radius) consisting of both Spidroin I and the less-ordered Spidroin II 1,2 .…”

Section: Introductionmentioning

confidence: 99%

“…The outer core (≈15% of the radius) is thought to consist mainly of the highly ordered protein Spidroin I, with the inner core (≈80% of the radius) consisting of both Spidroin I and the less-ordered Spidroin II 1,2 . The intrinsic disorder in Spidroin II occurs due to the presence of proline, which twists away from simple, ordered configurations 3 .…”

Section: Introductionmentioning

confidence: 99%

The critical role of water in spider silk and its consequence for protein mechanics

Brown

MacLeod

Amenitsch³

et al. 2011

Nanoscale

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Due to its remarkable mechanical and biological properties, there is considerable interest in understanding, and replicating, spider silk's stress-processing mechanisms and structure-function relationships. Here, we investigate the role of water in the nanoscale mechanics of the different regions in the spider silk fibre, and their relative contributions to stress processing. We propose that the inner core region, rich in spidroin II, retains water due to its inherent disorder, thereby providing a mechanism to dissipate energy as it breaks a sacrificial amide-water bond and gains order under strain, forming a stronger amide-amide bond. The spidroin I-rich outer core is more ordered under ambient conditions and is inherently stiffer and stronger, yet does not on its own provide high toughness. The markedly different interactions of the two proteins with water, and their distribution across the fibre, produce a stiffness differential and provide a balance between stiffness, strength and toughness under ambient conditions. Under wet conditions, this balance is destroyed as the stiff outer core material reverts to the behaviour of the inner core.3

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Composition and Hierarchical Organisation of a Spider Silk

Cited by 185 publications

References 48 publications

With great structure comes great functionality: Understanding and emulating spider silk

With great structure comes great functionality: Understanding and emulating spider silk

Increasing silk fibre strength through heterogeneity of bundled fibrils

The critical role of water in spider silk and its consequence for protein mechanics

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