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Recombinant DNA production of spider silk proteins.

Tokareva O, Michalczechen-Lacerda VA, Rech EL, Kaplan DL - Microb Biotechnol (2013)

Bottom Line: Moreover, silks are biocompatible and biodegradable protein-based materials.Recent advances in genetic engineering make it possible to produce recombinant silks in heterologous hosts, opening up opportunities for large-scale production of recombinant silks for various biomedical and material science applications.We review the current strategies to produce recombinant spider silks.

View Article: PubMed Central - PubMed

Affiliation: Department of Biomedical Engineering, Tufts University, Medford, MA, 02155, USA.

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Related in: MedlinePlus

A. An adult female orb weaver spider Nephila clavipes and her web.B. Schematic overview of N. clavipes web composed of three different spider silk proteins and their structures. The coloured boxes indicate the structural motifs in silk proteins. An empty box marked ‘?’ indicates that the secondary structure of the ‘spacer’ region is unknown. Note: MaSp1 or MaSp2: major ampullate spidroin 1 or 2; MiSp1 and 2: minor ampullate spidroin1 and 2; Flag: flagelliform protein. The photo was taken by Olena and Artem Tokarev in the Florida Keys.
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fig01: A. An adult female orb weaver spider Nephila clavipes and her web.B. Schematic overview of N. clavipes web composed of three different spider silk proteins and their structures. The coloured boxes indicate the structural motifs in silk proteins. An empty box marked ‘?’ indicates that the secondary structure of the ‘spacer’ region is unknown. Note: MaSp1 or MaSp2: major ampullate spidroin 1 or 2; MiSp1 and 2: minor ampullate spidroin1 and 2; Flag: flagelliform protein. The photo was taken by Olena and Artem Tokarev in the Florida Keys.

Mentions: Spider silks have been a focus of research for almost two decades due to their outstanding mechanical and biophysical properties. Spider silks are remarkable natural polymers that consist of three domains: a repetitive middle core domain that dominates the protein chain, and non-repetitive N-terminal and C-terminal domains. The large core domain is organized in a block copolymer-like arrangement, in which two basic sequences, crystalline [poly(A) or poly(GA)] and less crystalline (GGX or GPGXX) polypeptides alternate. At least seven different types of silk proteins are known for one orb-weaver species of spider (Lewis, 2006a). Silks differ in primary sequence, physical properties and functions (Hu et al., 2006). For example, dragline silks used to build frames, radii and lifelines are known for outstanding mechanical properties including strength, toughness and elasticity (Gosline et al., 1984). On an equal weight basis, spider silk has a higher toughness than steel and Kevlar (Vepari and Kaplan, 2007; Heim et al., 2009). Flageliform silk found in capture spirals has extensibility of up to 500%. Minor ampullate silk, which is found in auxiliary spirals of the orb-web and in prey wrapping, possesses high toughness and strength almost similar to major ampullate silks, but does not supercontract in water. Figure 1 depicts the location and structural elements of MaSp, MiSp and Flag silks.


Recombinant DNA production of spider silk proteins.

Tokareva O, Michalczechen-Lacerda VA, Rech EL, Kaplan DL - Microb Biotechnol (2013)

A. An adult female orb weaver spider Nephila clavipes and her web.B. Schematic overview of N. clavipes web composed of three different spider silk proteins and their structures. The coloured boxes indicate the structural motifs in silk proteins. An empty box marked ‘?’ indicates that the secondary structure of the ‘spacer’ region is unknown. Note: MaSp1 or MaSp2: major ampullate spidroin 1 or 2; MiSp1 and 2: minor ampullate spidroin1 and 2; Flag: flagelliform protein. The photo was taken by Olena and Artem Tokarev in the Florida Keys.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC3815454&req=5

fig01: A. An adult female orb weaver spider Nephila clavipes and her web.B. Schematic overview of N. clavipes web composed of three different spider silk proteins and their structures. The coloured boxes indicate the structural motifs in silk proteins. An empty box marked ‘?’ indicates that the secondary structure of the ‘spacer’ region is unknown. Note: MaSp1 or MaSp2: major ampullate spidroin 1 or 2; MiSp1 and 2: minor ampullate spidroin1 and 2; Flag: flagelliform protein. The photo was taken by Olena and Artem Tokarev in the Florida Keys.
Mentions: Spider silks have been a focus of research for almost two decades due to their outstanding mechanical and biophysical properties. Spider silks are remarkable natural polymers that consist of three domains: a repetitive middle core domain that dominates the protein chain, and non-repetitive N-terminal and C-terminal domains. The large core domain is organized in a block copolymer-like arrangement, in which two basic sequences, crystalline [poly(A) or poly(GA)] and less crystalline (GGX or GPGXX) polypeptides alternate. At least seven different types of silk proteins are known for one orb-weaver species of spider (Lewis, 2006a). Silks differ in primary sequence, physical properties and functions (Hu et al., 2006). For example, dragline silks used to build frames, radii and lifelines are known for outstanding mechanical properties including strength, toughness and elasticity (Gosline et al., 1984). On an equal weight basis, spider silk has a higher toughness than steel and Kevlar (Vepari and Kaplan, 2007; Heim et al., 2009). Flageliform silk found in capture spirals has extensibility of up to 500%. Minor ampullate silk, which is found in auxiliary spirals of the orb-web and in prey wrapping, possesses high toughness and strength almost similar to major ampullate silks, but does not supercontract in water. Figure 1 depicts the location and structural elements of MaSp, MiSp and Flag silks.

Bottom Line: Moreover, silks are biocompatible and biodegradable protein-based materials.Recent advances in genetic engineering make it possible to produce recombinant silks in heterologous hosts, opening up opportunities for large-scale production of recombinant silks for various biomedical and material science applications.We review the current strategies to produce recombinant spider silks.

View Article: PubMed Central - PubMed

Affiliation: Department of Biomedical Engineering, Tufts University, Medford, MA, 02155, USA.

Show MeSH
Related in: MedlinePlus