Isolation of a clone encoding a second dragline silk fibroin. Nephila clavipes dragline silk is a two-protein fiber.

Hinman, Michael; Lewis, Randy

doi:10.1016/s0021-9258(18)41777-2

Cited by 467 publications

(258 citation statements)

References 28 publications

Supporting

Mentioning

246

Contrasting

Order By: Relevance

“…Since the content of β-sheet structures was rising during the drying process, water loss and drying can be interpreted as the key triggering mechanism for crystallization. [21,[40][41][42] These observations are in agreement with complementary RAMAN spectroscopy measurements to determine the conformationally sensitive amide I signal which has been dominantly assigned to β-sheet structures with an emerging peak at a wavenumber of 1657 cm -1 . [43,44] Also, performing polarized microscopy of the skin demonstrated an increase in the birefringence of the samples over time indicative of conformational conversion and evolution of β-sheet motifs.…”

Section: Structural Evolution Of Skinsupporting

confidence: 83%

Interfacial crystallization and supramolecular self-assembly of spider silk inspired protein at the water-air interface

Mohammadi

Zemke

Wagermaier

2021

Preprint

View full text Add to dashboard Cite

Macromolecular assembly into complex morphologies and architectural shapes is an area of fundamental research and technological innovation. In this work, we investigate the self-assembly process of recombinantly produced protein inspired by spider silk (spidroin). To elucidate the first steps of the assembly process we looked into highly concentrated and viscous pendant droplets of this protein in air. We show how the protein self-assembles and crystallizes at the water-air interface into a relatively thick and highly elastic skin. Using time-resolved in-situ synchrotron x-ray scattering measurements during the drying process, we showed that the skin evolved to contain a high β-sheet amount over time. We also found that β-sheet formation strongly depended on protein concentration and relative humidity. These had a strong influence not only on the amount but also on the ordering of these structures during the β-sheet formation process. We also showed how the skin around pendant droplets can serve as a reservoir for attaining liquid-liquid phase separation and coacervation from the dilute protein solution. Essentially, this study shows a new assembly route which could be optimized for the synthesis of new materials from a dilute protein solution and determine the properties of the final products.

show abstract

Section: Structural Evolution Of Skinsupporting

confidence: 83%

Interfacial crystallization and supramolecular self-assembly of spider silk inspired protein at the water-air interface

Mohammadi

Zemke

Wagermaier

2021

Preprint

View full text Add to dashboard Cite

show abstract

“…This gradually resulted in the emergence of the two visible peaks towards the last scans. A sharp peak between 4 and 5 Å, with the maximum peak intensity at around 4.5 Å, is known to correspond to β-sheet interstrand spacing, as described previously, by combining experimental and computational simulation [ 19 , 38 , 39 , 40 ], A broader peak appeared between 8.5 and 11 Å, with its maximum intensity at 10.6 Å. This spacing is commonly assigned to β-sheet interspacing.…”

Section: Resultsmentioning

confidence: 59%

“…This spacing is commonly assigned to β-sheet interspacing. As the content of β-sheet structures was rising during the drying process, water loss and drying can be interpreted as the key triggering mechanism for crystallization [ 18 , 38 , 39 , 40 ]. These observations are in agreement with complementary RAMAN spectroscopy measurements to determine the conformationally sensitive amide I signal which has been dominantly assigned to β-sheet structures with an emerging peak at a wavenumber of 1657 cm −1 ( Figure 3 B) [ 41 , 42 ].…”

Section: Resultsmentioning

confidence: 99%

Interfacial Crystallization and Supramolecular Self-Assembly of Spider Silk Inspired Protein at the Water-Air Interface

2021

View full text Add to dashboard Cite

Macromolecular assembly into complex morphologies and architectural shapes is an area of fundamental research and technological innovation. In this work, we investigate the self-assembly process of recombinantly produced protein inspired by spider silk (spidroin). To elucidate the first steps of the assembly process, we examined highly concentrated and viscous pendant droplets of this protein in air. We show how the protein self-assembles and crystallizes at the water–air interface into a relatively thick and highly elastic skin. Using time-resolved in situ synchrotron X-ray scattering measurements during the drying process, we showed that the skin evolved to contain a high β-sheet amount over time. We also found that β-sheet formation strongly depended on protein concentration and relative humidity. These had a strong influence not only on the amount, but also on the ordering of these structures during the β-sheet formation process. We also showed how the skin around pendant droplets can serve as a reservoir for attaining liquid–liquid phase separation and coacervation from the dilute protein solution. Essentially, this study shows a new assembly route which could be optimized for the synthesis of new materials from a dilute protein solution and determine the properties of the final products.

show abstract

“…The glycine, glutamine, alanine and proline composition from spun MA silk is considered an indicator of its physical properties in accordance with a twospidroin (MaSp) model developed for the model spider, Nephila clavipes [15,16]. The model suggests that MA silk is a product of the relative expression of twospidroins, MaSp1 and MaSp2, which differ in amino acid composition and mechanical properties.…”

Section: Introductionmentioning

confidence: 97%

Post-secretion processing influences spider silk performance

Blamires

Blackledge

et al. 2012

J. R. Soc. Interface.

View full text Add to dashboard Cite

Phenotypic variation facilitates adaptations to novel environments. Silk is an example of a highly variable biomaterial. The two-spidroin (MaSp) model suggests that spider major ampullate (MA) silk is composed of two proteins-MaSp1 predominately contains alanine and glycine and forms strength enhancing β-sheet crystals, while MaSp2 contains proline and forms elastic spirals. Nonetheless, mechanical properties can vary in spider silks without congruent amino acid compositional changes. We predicted that post-secretion processing causes variation in the mechanical performance of wild MA silk independent of protein composition or spinning speed across 10 species of spider. We used supercontraction to remove post-secretion effects and compared the mechanics of silk in this 'ground state' with wild native silks. Native silk mechanics varied less among species compared with 'ground state' silks. Variability in the mechanics of 'ground state' silks was associated with proline composition. However, variability in native silks did not. We attribute interspecific similarities in the mechanical properties of native silks, regardless of amino acid compositions, to glandular processes altering molecular alignment of the proteins prior to extrusion. Such post-secretion processing may enable MA silk to maintain functionality across environments, facilitating its function as a component of an insect-catching web.

show abstract

Isolation of a clone encoding a second dragline silk fibroin. Nephila clavipes dragline silk is a two-protein fiber.

Cited by 467 publications

References 28 publications

Interfacial crystallization and supramolecular self-assembly of spider silk inspired protein at the water-air interface

Interfacial crystallization and supramolecular self-assembly of spider silk inspired protein at the water-air interface

Interfacial Crystallization and Supramolecular Self-Assembly of Spider Silk Inspired Protein at the Water-Air Interface

Post-secretion processing influences spider silk performance

Contact Info

Product

Resources

About