Abstract:
A recombinant fusion protein is comprising a spider silk fragment and a cyclic RGD cell-binding motif with selectivity for integrins, such as for α5β1 integrins. The fusion protein is useful as a cell scaffold material and for the cultivation of cells displaying integrins on their cell surface.
Abstract:
A method of producing a desired non-spidroin protein or polypeptide is comprising the steps of expressing in a suitable host a fusion protein, obtaining a mixture containing the fusion protein, and optionally isolating the fusion protein. The fusion protein is comprising at least one solubility-enhancing moiety which is derived from the N-terminal (NT) fragment of a spider silk protein. It is further comprising at least one moiety which is a desired non-spidroin protein or polypeptide. Each solubility-enhancing moiety is linked directly or indirectly to the desired protein or polypeptide moiety.
Abstract:
A recombinant fusion protein comprising the moieties Band CT is provided. B is a non-spidroin moiety which provides the capacity of selective interaction with an organic target. 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. The fusion protein is not comprising any moiety derived from the repetitive fragment of a spider silk protein.
Abstract:
A method for producing macroporous scaffolds which are useful in bone generation is provided. A liquid phase which is an aqueous solution of a non-denatured silk protein is subjected to mechanical foaming. A mineral phase comprising α-tricalcium phosphate (α-TCP) with hydroxyapatite (HA) is blended into the foamed liquid phase during continued mechanical foaming, thereby forming a macroporous paste. The macroporous paste is stabilized into a desired shape. The stabilized, shaped porous paste is mineralized into a macroporous calcium-deficient hydroxyapatite (CDHA)-based scaffold.
Abstract:
A protein comprising a moiety of 100-160 amino acid residues having at least 70% identity with the N-terminal (NT) fragment of a spider silk protein, wherein the amino acid residue corresponding to position 40 in NT is selected from the group consisting of Lys, Arg and His; and wherein the amino acid residue corresponding to position 65 in NT is selected from the group consisting of Asp and Glu, is useful as a moiety in a fusion protein for enhancing the solubility of another moiety in the fusion protein, which is a desired protein or polypeptide.
Abstract:
A recombinant fusion protein is comprising a spider silk fragment and a cyclic RGD cell-binding motif with selectivity for integrins, such as for α5β1 integrins. The fusion protein is useful as a cell scaffold material and for the cultivation of cells displaying integrins on their cell surface.
Abstract:
A cell scaffold material is manufactured by providing an aqueous solution of a silk protein capable of assembling into a water-insoluble macrostructure. The silk protein is mixed with eukaryotic cells, and the silk protein is assembled into a water-insoluble macrostructure in the presence of the cells, thereby forming a scaffold material for cultivating the cells. The cells can be grown integrated with the scaffold material under conditions suitable for cell culture.
Abstract:
A protein comprising a moiety of 100-160 amino acid residues having at least 70% identity with the N-terminal (NT) fragment of a spider silk protein, wherein the amino acid residue corresponding to position 40 in NT is selected from the group consisting of Lys, Arg and His; and wherein the amino acid residue corresponding to position 65 in NT is selected from the group consisting of Asp and Glu, is useful as a moiety in a fusion protein for enhancing the solubility of another moiety in the fusion protein, which is a desired protein or polypeptide.
Abstract:
A recombinant fusion protein comprising the moieties Band CT, and optionally REP, wherein B is comprising at least one immunoglobulin fragment, which provides the capacity of selective interaction with an organic target; 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; and REP is a moiety of from 70 to 300 amino acid residues and is derived from the repetitive fragment of a spider silk protein.
Abstract:
A recombinant fusion protein comprising the moieties B and CT is provided. B is a non-spidroin moiety which provides the capacity of selective interaction with an organic target. 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. The fusion protein is not comprising any moiety derived from the repetitive fragment of a spider silk protein.