Cellular and Molecular Life Sciences

, Volume 68, Issue 2, pp 169–184 | Cite as

Spider silk proteins: recent advances in recombinant production, structure–function relationships and biomedical applications

  • Anna Rising
  • Mona Widhe
  • Jan Johansson
  • My Hedhammar


Spider dragline silk is an outstanding material made up of unique proteins—spidroins. Analysis of the amino acid sequences of full-length spidroins reveals a tripartite composition: an N-terminal non-repetitive domain, a highly repetitive central part composed of approximately 100 polyalanine/glycine rich co-segments and a C-terminal non-repetitive domain. Recent molecular data on the terminal domains suggest that these have different functions. The composite nature of spidroins allows for recombinant production of individual and combined regions. Miniaturized spidroins designed by linking the terminal domains with a limited number of repetitive segments recapitulate the properties of native spidroins to a surprisingly large extent, provided that they are produced and isolated in a manner that retains water solubility until fibre formation is triggered. Biocompatibility studies in cell culture or in vivo of native and recombinant spider silk indicate that they are surprisingly well tolerated, suggesting that recombinant spider silk has potential for biomedical applications.


Spidroin Protein structure Recombinant protein production Biomaterial Protein self-assembly Biocompatibility 



Araneus diadematus fibroin




Major ampullate spidroin


Spider silk protein



We are grateful to Prof. Wilhelm Engström for introducing spidroin research at our department. Financial support from the Swedish Research Council, Formas, Vinnova, Spiber Technologies AB, and the EU Commission is gratefully acknowledged.


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Copyright information

© Springer Basel AG 2010

Authors and Affiliations

  • Anna Rising
    • 1
  • Mona Widhe
    • 1
  • Jan Johansson
    • 1
  • My Hedhammar
    • 1
  1. 1.Department of Anatomy Physiology and Biochemistry, The Biomedical CentreSwedish University of Agricultural SciencesUppsalaSweden

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