Molecular mechanism of spider silk elasticity

Dong, Zhengyu; Lewis, Randolph V.; Middaugh, C. Russell

doi:10.1016/0003-9861(91)90262-h

Cited by 88 publications

(61 citation statements)

References 15 publications

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“…Thereafter, the samples were washed several times in 0.1 M cacodylate buffer and postfixed for 2 h in 1% OsO 4 , washed several times in the same buffer, and stored overnight in 70% ethanol. On the next day, samples were dehydrated in a graded series ethanol up to 100%.…”

Section: Transmission Electron Microscopymentioning

confidence: 99%

Glycoproteins and skin‐core structure in Nephila clavipes spider silk observed by light and electron microscopy

2000

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Summary: Microscopical imaging of natural, unstressed draglines or of untreated bulk samples showed two types or threads with diameters of either ~ 1-2 µm or 4-5 µm, which could be identified as products of the minor or major ampullate glands. The threads had a circular profile in serial cross sections and are surrounded by a thin outer layer of a different material within the section. Such fibrillar configurations were also found in untreated threads or in the same serial sections of transmission electron microscopy (TEM) samples by means of the special technique of laser scanning microscopy. In TEM slides, numerous cavities with the same circular profile were detectable, and the length of these cavities is variable from 40-300 nm. The threads are oriented parallel and twisted around themselves to construct a double thread. In the interface between the two single threads, bridge-like structures are prominent. The single untreated thread consists of cylindrical fibers with a diameter of approximately 1-1.5 µm. Apparently more than eight fibers are within a thread and each fiber is composed of a great number of fibrils with a diameter of about 150 nm. The surface of threads is coated with a characteristic layer ~150-250 nm thick that contains glycoproteins. These were demonstrated for the first time by labeling with concanavalin A lectin-gold complex and are dependent on the diameter and length of the thread. The same substances could also be detected inside the single thread. The skin can be removed completely or partially by mechanical treatment, or by washing with phosphatebuffered saline or trypsin.

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Section: Transmission Electron Microscopymentioning

confidence: 99%

Glycoproteins and skin‐core structure in Nephila clavipes spider silk observed by light and electron microscopy

2000

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“…Although it has been suggested that the chemical composition ofsilks spun by spiders is much less variable than that ofsilks produced by larval insects (Rudall and Kenchington 1971), almost all research on the molecular, structural, and mechanical properties of spider silk has been completed on the support and viscid threads spun by fewer than 15 species of orb spinners (Lucas et al 1955;Zemlin 1968;Denny 1976;Wainwright et al 1976;Work 1977Work , 1981Work , 1985Gosline et al 1984;Craig 1987;Vollrath and Edmonds 1989;Xu and Lewis 1990;Dong et al 1991;Beckwith 1991;Hinman and Lewis 1992). However, the orb-spinning spiders and their close relatives (the Araneoidea) include only about onethird of all described spiders.…”

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confidence: 99%

Evolutionary Shifts in the Spectral Properties of Spider Silks

1994

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Abstract.-We measured the reflectance properties ofunpigmented silks spun by a systematic array of primitive (Deinopoidea) and derived (Araneoidea) aerial, web-spinning spiders, as well as silks spun by Araneomorphae and Mygalomorphae spiders that do not spin aerial webs. Our data show that all of the primitive aerial web spinners produce catching silks with a spectral peak in the ultraviolet (UV), and cladistic analysis suggests that high UV reflection is the primitive character state for silk spectral properties. In contrast, all of the derived aerial web spinners produce silks that are spectrally flat or characterized by reduced reflectance in the UV. Correlated with the evolution of these catching silks is a 37-fold increase in species number and apparent habitat expansion. This suggests that the unique silk proteins spun by the araneoids have been important to their ecological and evolutionary diversity.

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“…The major and minor ampullate silks are both very strong and at least one protein (MaSp1 and 2; MiSp1 and 2) in each silk contains the (GA) n /An β-sheet module (Hinman et al, 2000). The modules (GGX) n (where X = L, Q, R, or Y, depending on the silk) and (GPGXX) n (XX representing GA, GS, GY, or QQ) adopt less ordered conformations, most likely 3 10 -helices and turns, essential for fiber extensibility (Dong et al, 1991;Bram et al, 1997;Hayashi and Lewis, 2001;Rising et al, 2005). Flag silk, produced by the flagelliform gland, can have an elasticity of more than 200%, allowing more than double extension, and has the GPGXX module repeated up to 63 times in each repetitive unit (Hayashi and Lewis, 1998).…”

Section: Araneomorphae Silksmentioning

confidence: 99%

Review Protein families, natural history and biotechnological aspects of spider silk

Bittencourt¹,

Oliveira²,

Prosdocimi³

et al. 2012

Genet. Mol. Res.

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ABSTRACT. Spiders are exceptionally diverse and abundant organisms in terrestrial ecosystems and their evolutionary success is certainly related to their capacity to produce different types of silks during their life cycle, making a specialized use on each of them. Presenting particularly tandemly arranged amino acid repeats, silk proteins (spidroins) have mechanical properties superior to most synthetic or natural high-performance fibers, which makes them very promising for biotechnology industry, with putative applications in the production of new biomaterials. During the evolution of spider species, complex behaviors of web production and usage have been coupled with anatomical specialization of spinning glands. Spiders retaining ancestral characters, such as the ones belonging to the Mygalomorph group, present simpler sorts of webs used mainly to build burrows and egg sacs, and their silks are produced by globular undifferentiated spinning glands. In contrast, Araneomorphae spiders have a complex spinning apparatus, presenting up to seven morphologically distinct glands, capable to Protein family, history and biotechnology of spider silk produce a more complex set of silk polymers with different degrees of rigidness and elasticity associated with distinct behaviors. Aiming to provide a discussion involving a number of spider silks' biological aspects, in this review we present descriptions of members from each family of spidroin identified from five spider species of the Brazilian biodiversity, and an evolutionary study of them in correlation with the anatomical specialization of glands and spider's spinning behaviors. Due to the biotechnological importance of spider silks for the production of new biomaterials, we also discuss about the new possible technical and biomedical applications of spider silks and the current status of it.

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Molecular mechanism of spider silk elasticity

Cited by 88 publications

References 15 publications

Glycoproteins and skin‐core structure in Nephila clavipes spider silk observed by light and electron microscopy

Glycoproteins and skin‐core structure in Nephila clavipes spider silk observed by light and electron microscopy

Evolutionary Shifts in the Spectral Properties of Spider Silks

Review Protein families, natural history and biotechnological aspects of spider silk

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