G01N2800/7047

Systems and methods for binding amyloid fibrils using fluorescent protein

Methods and systems directed to monitoring for the presence or progression of amyloid diseases via detection of amyloid fibrils in a sample from an individual are disclosed. An individual, or sample from an individual, is treated with a reagent including a fluorescent protein. The fluorescent protein in the reagent binds to amyloid fibrils present in the sample. Detecting a signal from fluorescent protein bound to the treated sample indicates the presence of amyloid fibrils in the sample and possible diagnosis of an amyloid disease. The presence and progression of an amyloid disease is monitored by quantifying signal intensity from samples taken over time. Treatment with a reagent including a fluorescent protein inhibits amyloid fibril formation by providing the reagent to an environment including amyloid monomers. The fluorescent protein binds to amyloid oligomers during the lag phase and/or elongation phase of amyloid fibril formation, preventing formation of mature amyloid fibrils.

Anti-PHF-Tau Antibodies and Uses Thereof

Monoclonal anti-PHF-tau antibodies and antigen-binding fragments thereof are described. Also described are nucleic acids encoding the antibodies, compositions comprising the antibodies, methods of producing the antibodies, and use of the antibodies for treating or preventing conditions such as tauopathies.

NEW TAU SPECIES

The invention relates to the identification of a new Tau species starting at residue Met11 (Met11-Tau) which is N-alpha-terminally acetylated form (N-alpha-acetyl-Met11-Tau species: Ac-Met11-Tau). Several monoclonal antibodies specific of this new Tau species have been developed. One of this antibody, 2H2/D11, was used in THY-Tau22 mouse model (that develops with age neurofibrillary degeneration (NFD) and memory deficits), and N-alpha-Ac-Met11-Tau species were clearly detected early in neurons displaying NFD on hippocampal brain sections while it is not reactive in hippocampus from elderly controls. Finally, by using ELISA sandwich specific of Ac-Met11-Tau species, Alzheimer Disease (AD) brain samples are clearly discriminated from human elderly control brains. Thus the invention relates to this new Tau species starting from the methionine residue at position 11 said methionine being N-alpha acetylated. The invention also relates to antibody that specifically binds this new tau species, a method of detection of this new Tau species and a method of diagnosis of Tauopathy disorder.

CYCLIC PEPTIDE SPECIFICALLY BINDING TO APOPTOTIC CELLS AND USE THEREOF

Provided is a cyclic peptide (cyclo [Cys-Gln-Arg-Pro-Pro-Arg-Cys] peptide) comprised of the amino acid sequence of SEQ ID NO: 2; and a composition for apoptotic cell detection, drug delivery or imaging, containing the same as an active ingredient. The cyclic peptide (cyclo [Cys-Gln-Arg-Pro-Pro-Arg-Cys] peptide has an excellent effect of binding to apoptotic cells, compared with a linear peptide thereof, thereby greatly facilitating the detection of apoptotic cells and the in vivo imaging of an affected part under apoptosis, while the detection and imaging signal shows a very high correlation in disease prognosis prediction. The cyclic peptide binds to an imaging material, early diagnosing a response of a drug for treating diseases associated with abnormal cell proliferation, and binds to a therapeutic material, selectively delivering a drug to tissues afflicted with Apoptosis-associated diseases.

METHOD FOR THE BODY FLUID-BASED NEURODEGENERATIVE DISEASE DIAGNOSIS USING HIGH SENSITIVE IMMUNOASSAY OF AGGREGATED PROTEINS BY PHOTOOXIDATION-INDUCED AMPLIFICATION
20170307638 · 2017-10-26 ·

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.

Monoclonal Antibodies Against Pathological Alpha-Synuclein, and Methods Using Same

The present disclosure provides monoclonal antibodies that bind α-Synuclein. In certain aspects, the antibodies preferentially bind to α-Synuclein fibrils over α-Synuclein monomer. In other aspects, the invention comprises a method of treating α-Synucleopathic disease in a subject, comprising administering any of the antibodies of the invention to the subject. In yet other aspects, the invention comprises methods of detecting α-Synuclein fibrils using any of the antibodies of the invention.

Alpha-Synuclein Detection Assay and Method for Diagnosing Alpha-Synucleinopathies

A method of detecting the presence of alpha-synuclein aggregation in a biological sample is provided whereby a biological sample is mixed with a reaction sample comprising a population of beads, a fluorophore adapted to bind to protein aggregates and to increase fluorescence when bound to protein aggregates, and alpha-synuclein or a fragment or variant thereof to form a reaction mixture, the reaction mixture is illuminated and at the same time incubated with intermittent agitation cycles, wherein a significant increase in the fluorescence of the reaction mixture during incubation is indicative of the presence of aggregates of alpha-synuclein in the biological sample. Method of diagnosing alpha-synucleinopathies such as Parkinson's disease or Dementia with Lewy Bodies.

Identification of immunoglobulin free light chains by mass spectrometry

This document relates to methods for identifying one or more immunoglobulin free light chains in a sample using mass spectrometry. For example, this document relates to a method for identifying one or more immunoglobulin free light chains in a sample that includes (a) providing a sample; (b) subjecting the sample to a mass spectrometry technique to obtain a mass spectrum of the sample; and (c) identifying the presence of the one or more immunoglobulin free light chains.

Anti-PHF-tau antibodies and uses thereof

Monoclonal anti-PHF-tau antibodies and antigen-binding fragments thereof are described. Also described are nucleic acids encoding the antibodies, compositions comprising the antibodies, methods of producing the antibodies and using the antibodies for treating or preventing conditions such as tauopathies.

Alpha-synuclein detection assay and method for diagnosing alpha- synucleinopathies

A method of detecting the presence of alpha-synuclein aggregation in a biological sample is provided whereby a biological sample is mixed with a reaction sample comprising a population of beads, a fluorophore adapted to bind to protein aggregates and to increase fluorescence when bound to protein aggregates, and alpha-synuclein or a fragment or variant thereof to form a reaction mixture, the reaction mixture is illuminated and at the same time incubated with intermittent agitation cycles, wherein a significant increase in the fluorescence of the reaction mixture during incubation is indicative of the presence of aggregates of alpha-synuclein in the biological sample. Method of diagnosing alpha-synucleinopathies such as Parkinson's disease or Dementia with Lewy Bodies.