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Identification and dynamics of polyglycine II nanocrystals in Argiope trifasciata flagelliform silk
Spider silks combine a significant number of desirable characteristics in one material, including large tensile strength and strain at breaking, biocompatibility, and the possibility of tailoring their properties. Major ampullate gland silk (MAS) is the most studied silk and their properties are exp...
Autores principales: | , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group
2013
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3808813/ https://www.ncbi.nlm.nih.gov/pubmed/24162473 http://dx.doi.org/10.1038/srep03061 |
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author | Perea, G. B. Riekel, C. Guinea, G. V. Madurga, R. Daza, R. Burghammer, M. Hayashi, C. Elices, M. Plaza, G. R. Pérez-Rigueiro, J. |
author_facet | Perea, G. B. Riekel, C. Guinea, G. V. Madurga, R. Daza, R. Burghammer, M. Hayashi, C. Elices, M. Plaza, G. R. Pérez-Rigueiro, J. |
author_sort | Perea, G. B. |
collection | PubMed |
description | Spider silks combine a significant number of desirable characteristics in one material, including large tensile strength and strain at breaking, biocompatibility, and the possibility of tailoring their properties. Major ampullate gland silk (MAS) is the most studied silk and their properties are explained by a double lattice of hydrogen bonds and elastomeric protein chains linked to polyalanine β-nanocrystals. However, many basic details regarding the relationship between composition, microstructure and properties in silks are still lacking. Here we show that this relationship can be traced in flagelliform silk (Flag) spun by Argiope trifasciata spiders after identifying a phase consisting of polyglycine II nanocrystals. The presence of this phase is consistent with the dominant presence of the –GGX– and –GPG– motifs in its sequence. In contrast to the passive role assigned to polyalanine nanocrystals in MAS, polyglycine II nanocrystals can undergo growing/collapse processes that contribute to increase toughness and justify the ability of Flag to supercontract. |
format | Online Article Text |
id | pubmed-3808813 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | Nature Publishing Group |
record_format | MEDLINE/PubMed |
spelling | pubmed-38088132013-10-28 Identification and dynamics of polyglycine II nanocrystals in Argiope trifasciata flagelliform silk Perea, G. B. Riekel, C. Guinea, G. V. Madurga, R. Daza, R. Burghammer, M. Hayashi, C. Elices, M. Plaza, G. R. Pérez-Rigueiro, J. Sci Rep Article Spider silks combine a significant number of desirable characteristics in one material, including large tensile strength and strain at breaking, biocompatibility, and the possibility of tailoring their properties. Major ampullate gland silk (MAS) is the most studied silk and their properties are explained by a double lattice of hydrogen bonds and elastomeric protein chains linked to polyalanine β-nanocrystals. However, many basic details regarding the relationship between composition, microstructure and properties in silks are still lacking. Here we show that this relationship can be traced in flagelliform silk (Flag) spun by Argiope trifasciata spiders after identifying a phase consisting of polyglycine II nanocrystals. The presence of this phase is consistent with the dominant presence of the –GGX– and –GPG– motifs in its sequence. In contrast to the passive role assigned to polyalanine nanocrystals in MAS, polyglycine II nanocrystals can undergo growing/collapse processes that contribute to increase toughness and justify the ability of Flag to supercontract. Nature Publishing Group 2013-10-28 /pmc/articles/PMC3808813/ /pubmed/24162473 http://dx.doi.org/10.1038/srep03061 Text en Copyright © 2013, Macmillan Publishers Limited. All rights reserved http://creativecommons.org/licenses/by-nc-nd/3.0/ This work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivs 3.0 Unported License. To view a copy of this license, visit http://creativecommons.org/licenses/by-nc-nd/3.0/ |
spellingShingle | Article Perea, G. B. Riekel, C. Guinea, G. V. Madurga, R. Daza, R. Burghammer, M. Hayashi, C. Elices, M. Plaza, G. R. Pérez-Rigueiro, J. Identification and dynamics of polyglycine II nanocrystals in Argiope trifasciata flagelliform silk |
title | Identification and dynamics of polyglycine II nanocrystals in Argiope trifasciata flagelliform silk |
title_full | Identification and dynamics of polyglycine II nanocrystals in Argiope trifasciata flagelliform silk |
title_fullStr | Identification and dynamics of polyglycine II nanocrystals in Argiope trifasciata flagelliform silk |
title_full_unstemmed | Identification and dynamics of polyglycine II nanocrystals in Argiope trifasciata flagelliform silk |
title_short | Identification and dynamics of polyglycine II nanocrystals in Argiope trifasciata flagelliform silk |
title_sort | identification and dynamics of polyglycine ii nanocrystals in argiope trifasciata flagelliform silk |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3808813/ https://www.ncbi.nlm.nih.gov/pubmed/24162473 http://dx.doi.org/10.1038/srep03061 |
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