Abstract: The present invention relates to a method for concentrating and/or purifying prion PrPSc proteins by contacting prion PrPSc proteins with sepharose under conditions that allow for the specific and high affinity binding of the sepharose to the prion PrPSc proteins and removing the unbound non-prion proteins from the sepharose, as well as the same method for removing prion PrPSc proteins from body fluids by contacting body fluids with sepharose under conditions that allow for the specific and high affinity binding of the sepharose to the prion PrPSc proteins and removing the body fluid from said sepharose.

Abstract: The present invention relates to a method for removing prion PrPSc proteins from biological material by contacting a biological material comprising prion PrPSc proteins with sepharose under conditions that allow for the specific and high affinity binding of the sepharose to the prion PrPSc proteins and removing the biological material from the sepharose wherein the biological material is selected from mammalian urine or a fraction thereof or from cell culture-derived materials. Another aspect of the present invention concerns the use of specific and high affinity sepharose for removing prion PrPSc proteins from biological material.

Abstract: The present invention relates to the use of milk or a derivative thereof for identifying prion proteins, preferably PrPSc prion proteins, in a mammal. The present invention is also directed to a method for identifying prion proteins, preferably PrPSc prion proteins, in mammals, comprising the step of contacting milk or a derivative thereof with an agent having high affinity and selectivity for prion proteins, preferably for PrPSc prion proteins. In addition, a further aspect the present invention concerns a method for removing PrPC and/or PrPSc prion proteins, preferably PrPSc prion proteins, from milk or a milk derivative wherein milk or a derivative thereof is contacted with sepharose, preferably sepharose comprising divalent immobilized metal ions.

Abstract: The invention relates to a mutant prion protein (PrP), the globular domain of which comprises an engineered second disulfide bond in a similar position as in the human doppel protein (hDpl). In an embodiment, the prion protein has an engineered extra disulfide bond in the presumed ‘factor X’ binding epitope and is accommodated with slight, strictly localized conformational changes to inhibit prion propagation in human and animals. Also disclosed is the use of a mutant prion protein (PrP), the globular domain of which comprises at least one engineered additional disulfide bond in a similar position as in the human doppel protein, or fragments thereof for therapeutic treatment or for the manufacture of a medicament for therapeutic treatment of proteins causing disease after a conformational transition, e.g. Tranmissible Spongiform Encephalopathy (TSE), variant forms of Creutzfeldt-Jakob disease (CJD), fatal familial insomnia (FFI), and Gerstmann-Sträussler-Scheinker syndrome (GSS) in human.

Abstract: The invention provides an alternative method of reversible aggregation and/or dissociation of polypeptides. Proteins or polypeptides according to the invention have an inherent aggregation capability, wherein the aggregation is an oligomerization of the polypeptide that is based on the presence and the strucuture of peptide repeats localized in a flexibly disordered domain of this polypeptide. The flexibly disordered domain comprising the peptide repeats preferrably is located in close proximity with the N-terminus of the protein amino acid sequence. Preferably, each of the peptide repeats has a sequence that comprises one to four identical octapeptides with the amino acid sequence: PHGGGWGQ. Preferred proteins are selected from the group comprising cellular prion proteins (PrPC) and engineered polypeptides or fusion proteins with a respective inherent reversible aggregation and dissociation capability.

Abstract: The invention relates to an in vitro method for inducing a conformational transition in proteins, whereas said conformational transition results in an increased content of &bgr;-sheet secondary structure, the method comprising the steps of:

Abstract: The present invention provides a chaperone polypeptide having an amino acid sequence selected from at least amino acid residues 230-271 but no more than residues 150-455 or 151-456 of a GroEL, sequence substantially as shown in FIG. 7, or a corresponding sequence of a substantially homologous chaperone polypeptide, or a modified, mutated or variant sequence thereof having chaperone activity.