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Uppsala, Sweden

Lewicka M.,Karolinska Institutet | Hermanson O.,Karolinska Institutet | Rising A.U.,Swedish University of Agricultural Sciences | Rising A.U.,Spiber Technologies AB | Rising A.U.,Karolinska Institutet
Biomaterials | Year: 2012

Neural stem cells (NSCs) have the capacity to differentiate into neurons, astrocytes, and oligodendrocytes. Accordingly, NSCs hold great promise in drug screening and treatment of several common diseases. However, a major obstacle in applied stem cell research is the limitation of synthetic matrices for culturing stem cells. The objective of this study was to evaluate the suitability of recombinant spider silk (4RepCT) matrices for growth of NSCs. NSCs isolated from the cerebral cortices of mid-gestation rat embryos were cultured on either 4RepCT matrices or conventional poly-L-ornithine and fibronectin (P + F) coated polystyrene plates. From 48 h of culture, no significant differences in cell proliferation or viability were detected in NSC cultures on 4RepCT compared to control matrices (polystyrene plates coated with P + F). The NSCs retained an undifferentiated state, displaying low or no staining for markers of differentiated cells. Upon stimulation NSCs grown on 4RepCT differentiated efficiently into neuronal and astrocytic cells to virtually the same degree as control cultures, but a slightly less efficient oligodendrocyte differentiation was noted. We suggest that recombinant spider silk matrices provide a functional microenvironment and represent a useful tool for the development of new strategies in neural stem cell research. © 2012 . Source


Patent
Spiber Technologies Ab | Date: 2011-10-25

A protein structure capable of selective interaction with an organic target is provided. The protein structure is a polymer comprising as a repeating structural unit a recombinant fusion protein that is capable of selective interaction with the organic target. The fusion protein is comprising the moieties B, REP and CT, and optionally NT. B is a non-spidroin moiety of more than 30 amino acid residues, which provides the capacity of selective interaction with the organic target. REP is a moiety of from 70 to 300 amino acid residues and is derived from the repetitive fragment of a spider silk protein. CT is a moiety of from 70 to 120 amino acid residues and is derived from the C-terminal fragment of a spider silk protein. NT is an optional moiety of from 100 to 160 amino acid residues and is derived from the N-terminal fragment of a spider silk protein. The fusion protein and protein structure thereof is useful as an affinity medium and a cell scaffold material.


Patent
Spiber Technologies Ab | Date: 2011-04-12

A method and a combination for the cultivation of eukaryotic cells are provided, as well as a method for preparation of eukaryotic cells. The methods comprise providing a sample of eukaryotic cells to be cultured, applying said sample to a cell scaffold material; and maintaining said cell scaffold material having cells applied thereto under conditions suitable for cell culture. The combination comprises eukaryotic cells and a cell scaffold material. The cell scaffold material comprises a polymer of a spider silk protein.


Patent
Spiber Technologies AB | Date: 2013-11-21

The invention provides an isolated major ampullate spidroin protein, which consists of from 150 to 420 amino acid residues and is defined by the formula REP-CT. REP is a repetitive, N-terminally derived protein fragment having from 80 to 300 amino acid residues. CT is a C-terminally derived protein fragment having from 70 to 120 amino acid residues. The invention further provides an isolated fusion protein consisting of a first protein fragment, which is a major ampullate spidroin protein, and a second protein fragment comprising a fusion partner and a cleavage agent recognition site. The first protein fragment is coupled via said cleavage agent recognition site to the fusion partner. The invention also provides a method of producing a major ampullate spidroin protein and polymers thereof.


Patent
Spiber Technologies Ab | Date: 2015-06-29

A protein structure capable of selective interaction with an organic target is provided. The protein structure is a polymer comprising as a repeating structural unit a recombinant fusion protein that is capable of selective interaction with the organic target. The fusion protein is comprising the moieties B, REP and CT, and optionally NT. B is a non-spidroin moiety of more than 30 amino acid residues, which provides the capacity of selective interaction with the organic target. REP is a moiety of from 70 to 300 amino acid residues and is derived from the repetitive fragment of a spider silk protein. CT is a moiety of from 70 to 120 amino acid residues and is derived from the C-terminal fragment of a spider silk protein. NT is an optional moiety of from 100 to 160 amino acid residues and is derived from the N-terminal fragment of a spider silk protein. The fusion protein and protein structure thereof is useful as an affinity medium and a cell scaffold material.

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