Strain Dependent Structural Changes of Spider Dragline Silk

Glišović, Anja; Vehoff, Thorsten; Davies, Richard J.; Salditt, Tim

doi:10.1021/ma070528p

Cited by 70 publications

(72 citation statements)

References 25 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…10 A Poisson's ratio of 0.35 was used to account for the compressibility of the disordered domains and restructuring under load. 53 Stiffness was varied to represent the elastic modulus of bulk silk in ambient conditions (10 GPa), 10 and repeated at 100 MPa, 500 MPa, and 100 GPa for comparison. The upper surface of the upper fibril was fixed in space.…”

Section: Experiments and Simulationmentioning

confidence: 99%

Rough Fibrils Provide a Toughening Mechanism in Biological Fibers

et al. 2012

View full text Add to dashboard Cite

Spider silk is a fascinating\ud natural composite material. Its combination\ud of strength and toughness is unrivalled in\ud nature, and as a result, it has gained considerable\ud interest from the medical, physics,\ud and materials communities. Most of this\ud attention has focused on the one to tens of\ud nanometer scale: predominantly the primary\ud (peptide sequences) and secondary (β sheets,\ud helices, and amorphous domains) structure, with some insights into tertiary structure (the\ud arrangement of these secondary structures) to describe the origins of the mechanical and\ud biological performance. Starting with spider silk, and relating our findings to collagen fibrils,\ud we describe toughening mechanisms at the hundreds of nanometer scale, namely, the fibril\ud morphology and its consequences for mechanical behavior and the dissipation of energy.\ud Under normal conditions, this morphology creates a nonslip fibril kinematics, restricting\ud shearing between fibrils, yet allowing controlled local slipping under high shear stress,\ud dissipating energy without bulk fracturing. This mechanism provides a relatively simple target\ud for biomimicry and, thus, can potentially be used to increase fracture resistance in synthetic\ud materials

show abstract

Section: Experiments and Simulationmentioning

confidence: 99%

Rough Fibrils Provide a Toughening Mechanism in Biological Fibers

et al. 2012

View full text Add to dashboard Cite

show abstract

“…The overall toughness of the fiber is comparable to the total energy of the hydrogen bonds formed within the amorphous and the crystalline phase. Breaking of the hydrogen bonds upon fiber stretching is irreversible in the amorphous phase and reversible in the crystalline phase (stick-slip phenomenon) and represents a plausible mechanism for energy dissipation [109][110][111][112][113].…”

Section: Adf4mentioning

confidence: 99%

Recombinant Spider Silks—Biopolymers with Potential for Future Applications

2011

View full text Add to dashboard Cite

Nature has evolved a range of materials that compete with man-made materials in physical properties; one of these is spider silk. Silk is a fibrous material that exhibits extremely high strength and toughness with regard to its low density. In this review we discuss the molecular structure of spider silk and how this understanding has allowed the development of recombinant silk proteins that mimic the properties of natural spider silks. Additionally, we will explore the material morphologies and the applications of these proteins. Finally, we will look at attempts to combine the silk structure with chemical polymers and how the structure of silk has inspired the engineering of novel polymers.

show abstract

“…Typical scattering distributions for both types of sample preparations are shown in Figure 9 as a function of parallel and vertical momentum transfer. More details on experimental procedures and on the sample preparation by forced silking can be found in [33,24].…”

Section: Experimental Scattering Functionmentioning

confidence: 99%

“…Using highly brilliant microfocused synchrotron radiation, diffraction patterns can be obtained not only on thick samples of fiber bundles, but also on a single fiber [18][19][20][21][22][23]. Singlefiber diffraction was then used under simultaneous controlled mechanical load in order to investigate changes of the molecular structure with increasing strain up to failure [24]. Note that single-fiber diffraction, where possible, is much better suited to correlate the structure to controlled mechanical load, since the strain distribution in bundles is intrinsically inhomogeneous, and the majority of load may be taken up by a small minority of fibers.…”

Section: Introductionmentioning

confidence: 99%

Diffraction from the β -sheet crystallites in spider silk

et al. 2008

View full text Add to dashboard Cite

Abstract.We analyze the wide-angle X-ray scattering from oriented spider silk fibers in terms of a quantitative scattering model, including both structural and statistical parameters of the β-sheet crystallites of spider silk in the amorphous matrix. The model is based on kinematic scattering theory and allows for rather general correlations of the positional and orientational degrees of freedom, including the crystallite's size, composition and dimension of the unit cell. The model is evaluated numerically and compared to experimental scattering intensities allowing us to extract the geometric and statistical parameters. We show explicitly that for the experimentally found mosaicity (width of the orientational distribution) intercrystallite effects are negligible and the data can be analyzed in terms of single-crystallite scattering, as is usually assumed in the literature.PACS. 81.07.Bc Nanocrystalline materials -87.15.-v Biomolecules: structure and physical properties -61.05.cc Theories of X-ray diffraction and scattering

show abstract

Strain Dependent Structural Changes of Spider Dragline Silk

Cited by 70 publications

References 25 publications

Rough Fibrils Provide a Toughening Mechanism in Biological Fibers

Rough Fibrils Provide a Toughening Mechanism in Biological Fibers

Recombinant Spider Silks—Biopolymers with Potential for Future Applications

Diffraction from the β -sheet crystallites in spider silk

Contact Info

Product

Resources

About