Abstract:
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 KEP-CT. KEP 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.
Abstract:
A recombinant spider silk protein, consisting of no more than 800 amino acids, comprising a set of domains arranged according to the formula (NT)-REP-CT, wherein: the optional NT-domain, if present, comprises a sequence of 100 to 160 amino-acid residues derived from the N-terminal domain of a spider silk protein; the REP-domain comprises a sequence of 30 to 600 amino acid residues derived from the repetitive segment of a spider silk protein; and the CT-domain comprises a sequence of 70 to 120 amino acid residues derived from the C-terminal domain of a spider silk protein selected from: a sequence of 72 to 110 amino acid residues derived from the C-terminal domain of a spider silk protein, wherein the sequence comprises at least 7 residues independently selected from K, R, E and D; a sequence having at least 85% identity to SEQ ID NO: 15 or any one of SEQ ID NOs: 62-65 or 67-73; and a sequence having at least 70% identity to SEQ ID NOs: 64 or any one of SEQ ID NOs: 62-65 or 67-73, wherein the sequence comprises at least 7 residues independently selected from K, R, E and D.
Abstract:
A method for manufacturing shaped polymers of surface-active macromolecules, in particular silk, is provided. The method is comprising the steps of: • a) depositing an aqueous solution of the surface-active macromolecules on a surface, wherein the aqueous solution of the surface-active macromolecules is deposited in the form of a droplet, and wherein the surface is a hydrophobic micropatterned surface adapted to prevent the aqueous solution from penetrating into the pattern and to receive the droplet of the aqueous solution of the surface-active macromolecules and retain its droplet state; and • b) forming shaped polymers of the surface-active macromolecules on the surface.
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 recombinant spider silk protein, consisting of no more than 800 amino acids, comprising a set of domains arranged according to the formula (NT)-REP-CT, wherein: the optional NT-domain, if present, comprises a sequence of 100 to 160 amino-acid residues derived from the N-terminal domain of a spider silk protein; the REP-domain comprises a sequence of 30 to 600 amino acid residues derived from the repetitive segment of a spider silk protein; and the CT-domain comprises a sequence of 70 to 120 amino acid residues derived from the C-terminal domain of a spider silk protein selected from: a sequence of 72 to 110 amino acid residues derived from the C-terminal domain of a spider silk protein, wherein the sequence comprises at least 7 residues independently selected from K, R, E and D; a sequence having at least 85% identity to SEQ ID NO: 15 or any one of SEQ ID NO:s 62-65 or 67-73; and a sequence having at least 70% identity to SEQ. ID NO: 64 or any one of SEQ ID NO:s 62-65 or 67-73, wherein the sequence comprises at least 7 residues independently selected from K, R, E and D. Solutions, polymers, uses and methods of manufacture thereof.
Abstract:
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.
Abstract:
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.
Abstract:
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.
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:
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.