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Recombinant Minimalist Spider Wrapping Silk Proteins Capable of Native-Like Fiber Formation
Spider silks are desirable biomaterials characterized by high tensile strength, elasticity, and biocompatibility. Spiders produce different types of silks for different uses, although dragline silks have been the predominant focus of previous studies. Spider wrapping silk, made of the aciniform prot...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2012
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3509139/ https://www.ncbi.nlm.nih.gov/pubmed/23209681 http://dx.doi.org/10.1371/journal.pone.0050227 |
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author | Xu, Lingling Rainey, Jan K. Meng, Qing Liu, Xiang-Qin |
author_facet | Xu, Lingling Rainey, Jan K. Meng, Qing Liu, Xiang-Qin |
author_sort | Xu, Lingling |
collection | PubMed |
description | Spider silks are desirable biomaterials characterized by high tensile strength, elasticity, and biocompatibility. Spiders produce different types of silks for different uses, although dragline silks have been the predominant focus of previous studies. Spider wrapping silk, made of the aciniform protein (AcSp1), has high toughness because of its combination of high elasticity and tensile strength. AcSp1 in Argiope trifasciata contains a 200-aa sequence motif that is repeated at least 14 times. Here, we produced in E. coli recombinant proteins consisting of only one to four of the 200-aa AcSp1 repeats, designated W(1) to W(4). We observed that purified W(2), W(3) and W(4) proteins could be induced to form silk-like fibers by shear forces in a physiological buffer. The fibers formed by W(4) were ∼3.4 µm in diameter and up to 10 cm long. They showed an average tensile strength of 115 MPa, elasticity of 37%, and toughness of 34 J cm(−3). The smaller W(2) protein formed fewer fibers and required a higher protein concentration to form fibers, whereas the smallest W(1) protein did not form silk-like fibers, indicating that a minimum of two of the 200-aa repeats was required for fiber formation. Microscopic examinations revealed structural features indicating an assembly of the proteins into spherical structures, fibrils, and silk-like fibers. CD and Raman spectral analysis of protein secondary structures suggested a transition from predominantly α-helical in solution to increasingly β-sheet in fibers. |
format | Online Article Text |
id | pubmed-3509139 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2012 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-35091392012-12-03 Recombinant Minimalist Spider Wrapping Silk Proteins Capable of Native-Like Fiber Formation Xu, Lingling Rainey, Jan K. Meng, Qing Liu, Xiang-Qin PLoS One Research Article Spider silks are desirable biomaterials characterized by high tensile strength, elasticity, and biocompatibility. Spiders produce different types of silks for different uses, although dragline silks have been the predominant focus of previous studies. Spider wrapping silk, made of the aciniform protein (AcSp1), has high toughness because of its combination of high elasticity and tensile strength. AcSp1 in Argiope trifasciata contains a 200-aa sequence motif that is repeated at least 14 times. Here, we produced in E. coli recombinant proteins consisting of only one to four of the 200-aa AcSp1 repeats, designated W(1) to W(4). We observed that purified W(2), W(3) and W(4) proteins could be induced to form silk-like fibers by shear forces in a physiological buffer. The fibers formed by W(4) were ∼3.4 µm in diameter and up to 10 cm long. They showed an average tensile strength of 115 MPa, elasticity of 37%, and toughness of 34 J cm(−3). The smaller W(2) protein formed fewer fibers and required a higher protein concentration to form fibers, whereas the smallest W(1) protein did not form silk-like fibers, indicating that a minimum of two of the 200-aa repeats was required for fiber formation. Microscopic examinations revealed structural features indicating an assembly of the proteins into spherical structures, fibrils, and silk-like fibers. CD and Raman spectral analysis of protein secondary structures suggested a transition from predominantly α-helical in solution to increasingly β-sheet in fibers. Public Library of Science 2012-11-28 /pmc/articles/PMC3509139/ /pubmed/23209681 http://dx.doi.org/10.1371/journal.pone.0050227 Text en © 2012 Xu et al http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited. |
spellingShingle | Research Article Xu, Lingling Rainey, Jan K. Meng, Qing Liu, Xiang-Qin Recombinant Minimalist Spider Wrapping Silk Proteins Capable of Native-Like Fiber Formation |
title | Recombinant Minimalist Spider Wrapping Silk Proteins Capable of Native-Like Fiber Formation |
title_full | Recombinant Minimalist Spider Wrapping Silk Proteins Capable of Native-Like Fiber Formation |
title_fullStr | Recombinant Minimalist Spider Wrapping Silk Proteins Capable of Native-Like Fiber Formation |
title_full_unstemmed | Recombinant Minimalist Spider Wrapping Silk Proteins Capable of Native-Like Fiber Formation |
title_short | Recombinant Minimalist Spider Wrapping Silk Proteins Capable of Native-Like Fiber Formation |
title_sort | recombinant minimalist spider wrapping silk proteins capable of native-like fiber formation |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3509139/ https://www.ncbi.nlm.nih.gov/pubmed/23209681 http://dx.doi.org/10.1371/journal.pone.0050227 |
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