Cellular and Molecular Life Sciences

, Volume 68, Issue 2, pp 169–184

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

Authors

  • Anna Rising
    • Department of Anatomy Physiology and Biochemistry, The Biomedical CentreSwedish University of Agricultural Sciences
  • Mona Widhe
    • Department of Anatomy Physiology and Biochemistry, The Biomedical CentreSwedish University of Agricultural Sciences
    • Department of Anatomy Physiology and Biochemistry, The Biomedical CentreSwedish University of Agricultural Sciences
  • My Hedhammar
    • Department of Anatomy Physiology and Biochemistry, The Biomedical CentreSwedish University of Agricultural Sciences
Review

DOI: 10.1007/s00018-010-0462-z

Cite this article as:
Rising, A., Widhe, M., Johansson, J. et al. Cell. Mol. Life Sci. (2011) 68: 169. doi:10.1007/s00018-010-0462-z

Abstract

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.

Keywords

SpidroinProtein structureRecombinant protein productionBiomaterialProtein self-assemblyBiocompatibility

Abbreviations

ADF

Araneus diadematus fibroin

LPS

Lipopolysaccharide

MaSp

Major ampullate spidroin

Spidroin

Spider silk protein

Copyright information

© Springer Basel AG 2010