Water extraction by the major ampullate duct during silk formation in the spider, Argiope aurantia Lucas

Tillinghast, Edward K.; Chase, Susan F.; Townley, Mark A.

doi:10.1016/0022-1910(84)90088-x

Cited by 63 publications

(47 citation statements)

References 10 publications

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“…Interestingly, in the spider, water is removed from the spinning solution before fiber formation. 55 It Structural Features of a Silk-Like Protein by NMR might be that water functions in some other capacity than as a solubilizing agent, occupying a separate phase and not penetrating the core of the hydrophobic semicrystalline blocks. Alternatively, water may have a dual functionality in silk processing, serving as a coacervate at high protein concentration and plasticizer at lower concentrations.…”

Section: Topology and Fold Of The Crgd-silk Mimeticmentioning

confidence: 99%

High‐resolution NMR characterization of a spider‐silk mimetic composed of 15 tandem repeats and a CRGD motif

McLachlan¹,

Mantz²,

Kaplan³

et al. 2008

Protein Science

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Multidimensional solution NMR spectroscopic techniques have been used to obtain atomic level information about a recombinant spider silk construct in hexafluoro-isopropanol (HFIP). The synthetic 49 kDa silk-like protein mimics authentic silk from Nephila clavipes, with the inclusion of an extracellular matrix recognition motif. 2D 1 H-15 N HSQC NMR spectroscopy reveals 33 cross peaks, which were assigned to amino acid residues in the semicrystalline repeat units. Signals from the amorphous segments in the primary sequence were weak and broad, suggesting that this region is highly dynamic and undergoing conformational exchange. An analysis of the deviations of the 13 C a , 13 C b , and 13 CO chemical shifts relative to the expected random coil values reveals two highly a-helical regions from amino acid 12-19 and 26-32, which comprise the polyalanine track and a GGLGSQ sequence. This finding is further supported by /-value analysis and sequential and medium-range NOE interactions. Pulsed field gradient NMR measurements indicate that the topology of the silk mimetic in HFIP is nonglobular. Moreover, the 3D 15 N-NOESY HSQC spectrum exhibits few long-range NOEs. Similar spectral features have been observed for repeat modules in other polypeptides and are characteristic of an elongated conformation. The results provide a residue-specific description of a silk sequence in nonaqueous solution and may be insightful for understanding the fold and topology of highly concentrated, stable silk before spinning. Additionally, the insights obtained may find application in future design and large-scale production and storage of synthetic silks in organic solvents.

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Section: Topology and Fold Of The Crgd-silk Mimeticmentioning

confidence: 99%

High‐resolution NMR characterization of a spider‐silk mimetic composed of 15 tandem repeats and a CRGD motif

McLachlan¹,

Mantz²,

Kaplan³

et al. 2008

Protein Science

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show abstract

“…However, silk spun from the same gland can also exhibit extreme variability, even at the intra-individual level (Madsen et al, 1999). Both the potential adaptive value and the mechanisms causing this variation are unclear (but see Tso et al, 2007;Boutry and Blackledge, 2008 applied on the silk (Knight and Vollrath, 1999) and changes in pH (Dicko et al, 2004), water (Tillinghast et al, 1984) and ion content within the spinning duct as well as variation of the ratio of the different proteins composing silk (Rising et al, 2005;Boutry and Blackledge, 2008). Understanding how spiders control silk properties through spinning is critical for industrial production of silk.…”

Section: Introductionmentioning

confidence: 99%

Biomechanical variation of silk links spinning plasticity to spider web function

Boutry

Blackledge

2009

Zoology

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“…Particularly noteworthy is that water is absorbed from the dope during its passage along the spinning duct (Kojic et al, 2004 andTillinghast et al, 1984), which increases the concentration of proteins and consequently increases the shear forces between the proteins in the dope due to strengthened hydrophobic interactions. This leads us to suggest that shear forces are likely to play a greater role than salt effects during the fiber spinning process in vivo ( Casem et al, 2002, Knight and Vollrath, 2002, Perez-Rigueiro et al, 2001aand Perez-Rigueiro et al, 2001b.…”

Section: Figure Optionsmentioning

confidence: 99%

The role of salt and shear on the storage and assembly of spider silk proteins

Eisoldt

Hardy

Heim

et al. 2010

Journal of Structural Biology

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Major ampullate silk fibers of orb web-weaving spiders have impressive mechanical properties due to the fact that the underlying proteins partially fold into helical/amorphous structures, yielding relatively elastic matrices that are toughened by anisotropic nanoparticulate inclusions (formed from stacks of β-sheets of the same proteins). In vivo the transition from soluble protein to solid fibers involves a combination of chemical and mechanical stimuli (such as ion exchange, extraction of water and shear forces). Here we elucidate the effects of such stimuli on the in vitro aggregation of engineered and recombinantly produced major ampullate silk-like proteins (focusing on structurefunction relationships with respect to their primary structures), and discuss their relevance to the storage and assembly of spider silk proteins in vivo.

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Water extraction by the major ampullate duct during silk formation in the spider, Argiope aurantia Lucas

Cited by 63 publications

References 10 publications

High‐resolution NMR characterization of a spider‐silk mimetic composed of 15 tandem repeats and a CRGD motif

High‐resolution NMR characterization of a spider‐silk mimetic composed of 15 tandem repeats and a CRGD motif

Biomechanical variation of silk links spinning plasticity to spider web function

The role of salt and shear on the storage and assembly of spider silk proteins

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