Spiber Technologies Ab

Kerstin Nordling

Anna Rising

My Hedhammar

Nina Kronqvist

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.

Charge-reversed N-terminal spider silk protein domain and uses thereof

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.

Production of proteins and polypeptides

A method of producing polymers of an isolated spider silk protein involves providing a solution of said spider silk protein in a liquid medium at pH 6.4 or higher and/or an ion composition that prevents polymerization of the spider silk protein. The properties of the liquid medium are adjusted to a pH of 6.3 or lower and an ion composition that allows polymerization of the spider silk protein. The spider silk protein is allowed to form polymers in the liquid medium, and the resulting spider silk protein polymers are isolated from the liquid medium. The resulting polymers are useful as fibers, films, foams, nets or meshes.

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Knivsta, Sweden

Kerstin Nordling