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Spider silks: recombinant synthesis, assembly, spinning, and engineering of synthetic proteins

Since thousands of years humans have utilized insect silks for their own benefit and comfort. The most famous example is the use of reeled silkworm silk from Bombyx mori to produce textiles. In contrast, despite the more promising properties of their silk, spiders have not been domesticated for larg...

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Detalles Bibliográficos
Autor principal: Scheibel, Thomas
Formato: Texto
Lenguaje:English
Publicado: BioMed Central 2004
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC534800/
https://www.ncbi.nlm.nih.gov/pubmed/15546497
http://dx.doi.org/10.1186/1475-2859-3-14
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author Scheibel, Thomas
author_facet Scheibel, Thomas
author_sort Scheibel, Thomas
collection PubMed
description Since thousands of years humans have utilized insect silks for their own benefit and comfort. The most famous example is the use of reeled silkworm silk from Bombyx mori to produce textiles. In contrast, despite the more promising properties of their silk, spiders have not been domesticated for large-scale or even industrial applications, since farming the spiders is not commercially viable due to their highly territorial and cannibalistic nature. Before spider silks can be copied or mimicked, not only the sequence of the underlying proteins but also their functions have to be resolved. Several attempts to recombinantly produce spider silks or spider silk mimics in various expression hosts have been reported previously. A new protein engineering approach, which combines synthetic repetitive silk sequences with authentic silk domains, reveals proteins that closely resemble silk proteins and that can be produced at high yields, which provides a basis for cost-efficient large scale production of spider silk-like proteins.
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spelling pubmed-5348002004-12-04 Spider silks: recombinant synthesis, assembly, spinning, and engineering of synthetic proteins Scheibel, Thomas Microb Cell Fact Review Since thousands of years humans have utilized insect silks for their own benefit and comfort. The most famous example is the use of reeled silkworm silk from Bombyx mori to produce textiles. In contrast, despite the more promising properties of their silk, spiders have not been domesticated for large-scale or even industrial applications, since farming the spiders is not commercially viable due to their highly territorial and cannibalistic nature. Before spider silks can be copied or mimicked, not only the sequence of the underlying proteins but also their functions have to be resolved. Several attempts to recombinantly produce spider silks or spider silk mimics in various expression hosts have been reported previously. A new protein engineering approach, which combines synthetic repetitive silk sequences with authentic silk domains, reveals proteins that closely resemble silk proteins and that can be produced at high yields, which provides a basis for cost-efficient large scale production of spider silk-like proteins. BioMed Central 2004-11-16 /pmc/articles/PMC534800/ /pubmed/15546497 http://dx.doi.org/10.1186/1475-2859-3-14 Text en Copyright © 2004 Scheibel; licensee BioMed Central Ltd.
spellingShingle Review
Scheibel, Thomas
Spider silks: recombinant synthesis, assembly, spinning, and engineering of synthetic proteins
title Spider silks: recombinant synthesis, assembly, spinning, and engineering of synthetic proteins
title_full Spider silks: recombinant synthesis, assembly, spinning, and engineering of synthetic proteins
title_fullStr Spider silks: recombinant synthesis, assembly, spinning, and engineering of synthetic proteins
title_full_unstemmed Spider silks: recombinant synthesis, assembly, spinning, and engineering of synthetic proteins
title_short Spider silks: recombinant synthesis, assembly, spinning, and engineering of synthetic proteins
title_sort spider silks: recombinant synthesis, assembly, spinning, and engineering of synthetic proteins
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC534800/
https://www.ncbi.nlm.nih.gov/pubmed/15546497
http://dx.doi.org/10.1186/1475-2859-3-14
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