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

Rising, Anna, Widhe, Mona, Johansson, Jan, Hedhammar, My
Cellular and molecular life sciences 2011 v.68 no.2 pp. 169-184
Araneae, amino acid composition, amino acid sequences, biocompatibility, cell culture, silk, silk proteins, structure-activity relationships, water solubility
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.