Alpha-sheet polypeptide multimers, and polypeptides for making multimers, compositions and medical devices including them, and their use for treating and diagnosing amyloid diseases or amyloid-associated diseases are disclosed.

The invention provides a method that gives direct information about the intervention of a potential drug on the secondary structure distribution of a targetbiomolecule, i.e., for a disease with misfolded protein, such as neurodegenerative diseases in a complex body fluid. The secondary structural change is monitored by vibrational spectroscopy. The method can be applied for prescreening of drug candidates for targeting of specific biomolecules. The effect of the drug on the secondary structure distribution is monitored label-free in real time and provides thereby direct information about the efficacy of the potential drug.

The invention provides anti-Tau antibodies and methods of using the same.

A method for the pre-amplification sample processing of a prion or other amyloid converting protein in a sample. A key feature of the assay is its ability to amplify and thus detect small quantities of the abnormally folded ‘seed’ forms of misfolded proteins. The assay also opens up the ability to quantify the amount of “seed” present. The methods facilitate the early detection of diseases associated with misfolded proteins, as well as assessment of therapies against these diseases. The method can detect amyloid seeding activity (prions) in blood samples, including the buffy coat cells harvested from pre-clinical and clinical subjects. These findings further enhance the ability to assess the longitudinal course of prion disease and the role hematogenous prions play in pathogenesis. We demonstrate the ability to detect prions in as few as 5×10.sup.5 buffy coat cells by lipase-iron oxide bead-RT-QuIC performed at 42° C. (LIQ42) in 79% of CWD-biopsy positive WTD, which increased to 100% when LIQ was performed at 55° C. (LIQ55). RT-QuIC assessment of PMCA (PQ) round 5 product revealed hematogenous prions in 92% of the WTD.

In an ex vivo method of diagnosing a disease associated with synaptic degeneration, a concentration of beta-synuclein in a cerebrospinal fluid (CSF) sample taken from a patient is determined by an enzyme-linked immunosorbent assay (ELISA).

The present invention relates to a chimeric protein comprising at least one human amyloid P component and at least one fragment of an Fc region of a human antibody, the human amyloid P component and the fragment of an Fc region with which it is associated being bound to each other by means of a hinge region.

Disclosed is a method for body fluid-based neurodegenerative disease diagnosis through high-sensitive immunoassay of aggregated proteins by photooxidation-induced amplification. The method according to the present disclosure provides an effect of quantitatively analyzing aggregated proteins in the form of oligomers or monomers which are present in trace amounts in a body fluid and measures normal or abnormal protein aggregation by detecting the aggregated proteins in the form of oligomers or monomers with high sensitivity by reaction of antibody-conjugated enzymes selectively bound to the aggregated proteins with substrates and photooxidation-induced amplification, thereby allowing accurate diagnosis of a neurodegenerative disease.

The invention provides anti-Tau antibodies and methods of using the same.

The present invention relates to anti-alpha-synuclein (anti-α-synuclein) antibodies and methods of using the same.

Prion peptides comprising prion epitopes and fusions thereof, that display enhanced immunogenicity are described. Also described are methods of treating and diagnosing prion disease.