Encyclopedia of Nanotechnology

Living Edition
| Editors: Bharat Bhushan

Spider Silk

  • Fritz VollrathEmail author
Living reference work entry
DOI: https://doi.org/10.1007/978-94-007-6178-0_269-2



Silks are animal fibers (or more rarely ribbons or sheets) of proteinageous biomaterials that are, by definition, extrusion spun [1]. While the evolutionary origins and taxonomic placement of silk feedstocks can differ widely across the arthropods, filaments can be surprisingly similar [2]. Capture silks are sticky materials depolying either nanoscale filaments or aqueous glycoprotein glues that have evolved from dry silks [3].


Silks are fascinating biological products and have evolved several times independently in the arthropods. Spiders and moths are the best-known and best-studied of silk spinners, but there are others ranging from mites to bees [2]. In each taxon the diversity of silks has evolved in only one ancestor but then radiated quickly (over millions of years) into many different types fit for the various purposes required by the animal – be it integration into a cocoon composite or use as a single safety...


Silk Fiber Silk Protein Spider Silk Dragline Silk Native Silk 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
This is a preview of subscription content, log in to check access.


  1. 1.
    Vollrath, F., Porter, D.: Silks as ancient models for modern polymers. Polymer 50, 5623–5632 (2009)CrossRefGoogle Scholar
  2. 2.
    Sutherland, T.D., Young, J., Weisman, S., Hayashi, C.Y., Merrit, D.: Insect silk: one name, many materials. Annu. Rev. Entomol. 55, 171–188 (2010)CrossRefGoogle Scholar
  3. 3.
    Brunetta, L., Craig, C.: Spider Silk: Evolution and 400 Million Years of Spinning, Waiting, Snagging, and Mating, pp. 1–229. Yale University Press, New Haven/London (2010)Google Scholar
  4. 4.
    Vollrath, F.: Spider webs and silks. Sci. Am. 266(3), 46–52 (1992)CrossRefGoogle Scholar
  5. 5.
    Fu, C., Shao, Z., Vollrath, F.: Animal silks: their structures, properties and artificial production. Chem. Commun. 43, 6515–6529 (2009)CrossRefGoogle Scholar
  6. 6.
    Omenetto, F., Kaplan, D.L.: New opportunities for an ancient material. Science 329, 528–531 (2010)CrossRefGoogle Scholar
  7. 7.
    Porter, D., Vollrath, F.: Silk as a biomimetic ideal for structural polymers. Adv. Mater. 21, 487–492 (2009)CrossRefGoogle Scholar
  8. 8.
    Harmer, A.M.T., Blackledge, T.A., Madin, J.S., Herberstein, M.E.: High-performance spider webs: integrating biomechanics, ecology and behaviour. J. R. Soc. Interface 8, 457–471 (2011)CrossRefGoogle Scholar
  9. 9.
    Vollrath, F., Porter, D., Dicko, C.: The structure of silk. In: Eichhorn, S.J., Hearlem, J.W.S., Jaffe, M., Kikutani, T. (eds.) Handbook of Textile Fibre Structure, vol. 2, pp. 146–198. Woodhead Publishing, Oxford/Cambridge, MA/New Delhi (2009)CrossRefGoogle Scholar
  10. 10.
    Vollrath, F., Knight, D.P.: Liquid crystal silk spinning in nature. Nature 410, 541–548 (2001)CrossRefGoogle Scholar
  11. 11.
    Aldo Leal-Egaña, A., Scheibel, T.: Silk-based materials for biomedical applications. Biotechnol. Appl. Biochem. 55, 155–167 (2010)CrossRefGoogle Scholar
  12. 12.
    Dicko, C., Porter, D., Vollrath, F.: Silk: relevance to amyloids. In: Riggaci, S., Bucciantini, M. (eds.) Functional Amyloid Aggregation, pp. 51–70. Research SignPost, Trivandrum (2010)Google Scholar
  13. 13.
    Porter, D., Vollrath, F.: The role of kinetics of water and amide bonding in protein stability. Soft. Matter. 4, 328–336 (2008)CrossRefGoogle Scholar
  14. 14.
    Holland, C., Vollrath, F.: Biomimetic principles of spider silk for high-performance fibres. Chapter 7. In: Ellison, M.S., Abbott, A.G. (eds.) Biologically Inspired Textiles. Woodhead Publishing, Cambridge, MA (2008)Google Scholar
  15. 15.
    Liu, Y., Sponner, A., Porter, D., Vollrath, F.: Proline and processing of spider silks. Biomacromolecules 9, 116–121 (2008)CrossRefGoogle Scholar
  16. 16.
    Porter, D.: Group Interaction Modelling of Polymers. Marcel Dekker, New York (1995)Google Scholar
  17. 17.
    Holland, C., Terry, E.A., Porter, D., Vollrath, F.: Rheological characterisation of native spider and silkworm dope. Nat. Mater. 5, 870–874 (2006)CrossRefGoogle Scholar
  18. 18.
    Spiess, K., Lammel, A., Scheibel, T.: Recombinant spider silk proteins for applications in biomaterials. Macromol. Biosci. 10, 998–1007 (2010)CrossRefGoogle Scholar
  19. 19.
    Holland, C., Vollrath, F., Ryan, A.J., Mykhaylyk, O.O.: Silk and synthetic polymers; reconciling 100 degrees of separation. Adv. Mater. 24, 105–109 (2012)CrossRefGoogle Scholar
  20. 20.
    Porter, D., Vollrath, F.: Water mediated proton hopping empowers proteins. Soft. Matter. 9, 643–646 (2013)CrossRefGoogle Scholar
  21. 21.
    Porter, D., Vollrath, F.: Water mobility, denaturation and the glass transition in proteins. Biochim. Biophys. Acta (BBA) Proteins Proteomics 1824, 785–791 (2012)CrossRefGoogle Scholar
  22. 22.
    Vollrath, F., Porter, D.: Spider silk as archetypal protein elastomer. Soft. Matter. 2(5), 377–385 (2006)CrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media Dordrecht 2015

Authors and Affiliations

  1. 1.Department of ZoologyUniversity of OxfordOxfordUK