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...
| Main Authors: | , , , |
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| Format: | Article |
| Language: | English |
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Public Library of Science (PLoS)
2012-01-01
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| Series: | PLoS ONE |
| Online Access: | http://europepmc.org/articles/PMC3509139?pdf=render |
| _version_ | 1818380968300380160 |
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| author | Lingling Xu Jan K Rainey Qing Meng Xiang-Qin Liu |
| author_facet | Lingling Xu Jan K Rainey Qing Meng Xiang-Qin Liu |
| author_sort | Lingling Xu |
| collection | DOAJ |
| 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. |
| first_indexed | 2024-12-14T02:27:06Z |
| format | Article |
| id | doaj.art-7d6fce8a4a0a478e80e722bd92604beb |
| institution | Directory Open Access Journal |
| issn | 1932-6203 |
| language | English |
| last_indexed | 2024-12-14T02:27:06Z |
| publishDate | 2012-01-01 |
| publisher | Public Library of Science (PLoS) |
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| series | PLoS ONE |
| spelling | doaj.art-7d6fce8a4a0a478e80e722bd92604beb2022-12-21T23:20:21ZengPublic Library of Science (PLoS)PLoS ONE1932-62032012-01-01711e5022710.1371/journal.pone.0050227Recombinant minimalist spider wrapping silk proteins capable of native-like fiber formation.Lingling XuJan K RaineyQing MengXiang-Qin LiuSpider 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.http://europepmc.org/articles/PMC3509139?pdf=render |
| spellingShingle | Lingling Xu Jan K Rainey Qing Meng Xiang-Qin Liu Recombinant minimalist spider wrapping silk proteins capable of native-like fiber formation. PLoS ONE |
| 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 |
| url | http://europepmc.org/articles/PMC3509139?pdf=render |
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