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Spider silk proteins: recent advances in recombinant production, structure-function relationships and biomedical applications
Department of Anatomy Physiology and Biochemistry, Temp Medical Centre, Swedish University of Agricultural Sciences, Uppsala .ORCID iD: 0000-0003-0140-419X
2011 (English)In: Cellular and Molecular Life Sciences (CMLS), ISSN 1420-682X, E-ISSN 1420-9071, Vol. 68, no 2, p. 169-84Article, review/survey (Refereed) Published
Abstract [en]

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.

Place, publisher, year, edition, pages
Springer, 2011. Vol. 68, no 2, p. 169-84
Keywords [en]
Amino Acid Sequence, Animals, *Biocompatible Materials, *Fibroins/chemistry/genetics/physiology, Humans, Molecular Sequence Data, Plants, Genetically Modified, Protein Structure, Tertiary, Recombinant Fusion Proteins/chemistry/genetics/physiology, Regenerative Medicine, Sequence Analysis, *Spiders, Structure-Activity Relationship
National Category
Biochemistry and Molecular Biology
Identifiers
URN: urn:nbn:se:kth:diva-250632ISI: 000285970400001PubMedID: 20668909Scopus ID: 2-s2.0-78651367978ISBN: 1420-9071 (Electronic) 1420-682X (Linking) OAI: oai:DiVA.org:kth-250632DiVA, id: diva2:1310593
Note

QC 20190617

Available from: 2019-04-30 Created: 2019-04-30 Last updated: 2019-06-17Bibliographically approved

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