The present invention provides the method to prevent or slow down the progression of degenerative diseases caused by membrane channel-forming peptides. For many of these diseases, there is no known treatment based on the etiology and pathogenesis of the corresponding disease. Until recently, there was no integrative theory explaining multiple symptoms and observations associated with such diseases. In response to this challenge, we developed the amyloid degradation toxicity theory of Alzheimer's disease (AD). Within this concept, the etiology of the disease is the formation of beta-amyloid fragments which form membrane channels. We claim that the stopping the production of toxic fragments by inhibiting biochemical pathways producing channel-forming fragments (for example, by protease inhibitors) will prevent or slow down the progression AD. Also, we claim that the same molecular mechanism is involved in multiple neurodegenerative diseases and diabetes type II, so the invented method can be used to treat them.

The present invention provides the method to prevent or slow down the progression of degenerative diseases caused by membrane channel-forming peptides. For many of these diseases, there is no known treatment based on the etiology and pathogenesis of the corresponding disease. Until recently, there was no integrative theory explaining multiple symptoms and observations associated with such diseases. In response to this challenge, we developed the amyloid degradation toxicity theory of Alzheimer's disease (AD). Within this concept, the etiology of the disease is the formation of beta-amyloid fragments which form membrane channels. We claim that the stopping the production of toxic fragments by inhibiting biochemical pathways producing channel-forming fragments (for example, by protease inhibitors) will prevent or slow down the progression AD. Also, we claim that the same molecular mechanism is involved in multiple neurodegenerative diseases and diabetes type II, so the invented method can be used to treat them.

Antibody for human amyloid beta. Antibody selectively binds human amyloid beta 42 peptide over human amyloid beta 40 peptide. Antibodies specific for amyloid beta 42 as therapeutic agents for binding amyloid beta 42 peptide and treating conditions associated with amyloidosis, such as Alzheimer's disease.

The present invention relates to a compound for use in the treatment or prevention of a liver disease, wherein the compound is a amyloid beta related protein, the amyloid beta related protein being selected from the group consisting of amyloid beta protein, a amyloid beta peptide derived therefrom, amyloid precursor protein (APP), a compound involved in the generation of an amyloid beta peptide from APP, or a compound inhibiting the degradation of the amyloid beta protein or of amyloid peptides derived therefrom.

Disclosed herein are compositions and methods for treating and preventing neurodegenerative diseases, such as Alzheimer's disease. In some embodiments, the composition comprises a peptide that disrupts the binding between PTPσ and APP, preventing β-amyloidogenic processing of APP without affecting other major substrates of β- and γ-secretases. Alternatively, in some embodiments, an antibody or a fragment of an antibody against PTPσ or APP may be used to disrupt the binding between PTPσ and APP. In some embodiments, the composition comprises compounds or enzymes, which restore perineuronal balance of PTPσ ligands CS and HS, thereby preventing abnormally increased β-amyloidogenic processing of APP. Compositions and methods disclosed herein can be used in combination to treat and prevent neurodegenerative diseases.

The present disclosure relates to compositions and methods for the production of antimicrobial amyloid compositions, and further relates to use of such antimicrobial preparations for the treatment of subjects having drug-resistant microbial infections. Advantageous and/or therapeutic amyloid oligomer immunodepletion methods are also disclosed.

In part, the disclosure relates to methods of treating fibrotic cancers by administering one or more Serum Amyloid Protein (SAP) agonists. In certain aspects, the method further comprises the conjoint administration of an anti-cancer therapeutic, e.g., a chemotherapeutic agent. In certain aspects, the disclosure relates to methods of treating myelofibrosis by administering an SAP agonist and optionally one or more anti-cancer therapeutic agents.

Methods and dosing regimens using alpha 7 acetylcholine nicotine receptor binding agents are provided to prevent or inhibit intracellular accumulation of amyloid in cells leading to inhibition or prevention of neuronal cell death. In addition, these methods and dosing regimens are coupled with methods and dosing regimens to reduce and/or prevent blood-brain barrier leakage of vascular-derived amyloid into the brain and/or methods and dosing regimens to reduce and/or prevent neuroinflammation to prevent and/or inhibit the progression of Alzheimer's disease and other forms of dementia and mild cognitive impairment. Also provided are methods for identifying individuals for this treatment.

Methods and dosing regimens using alpha 7 acetylcholine nicotine receptor binding agents are provided to prevent or inhibit intracellular accumulation of amyloid in cells leading to inhibition or prevention of neuronal cell death. In addition, these methods and dosing regimens are coupled with methods and dosing regimens to reduce and/or prevent blood-brain barrier leakage of vascular-derived amyloid into the brain and/or methods and dosing regimens to reduce and/or prevent neuroinflammation to prevent and/or inhibit the progression of Alzheimer's disease and other forms of dementia and mild cognitive impairment. Also provided are methods for identifying individuals for this treatment.

Here, we describe a minimalist approach to mimic the aggregation-prone modules within tau. We carried out a backbone residue scan and showed that amide N-amination completely abolishes the tendency of these peptides to self-aggregate, rendering them soluble mimics of ordered β-strands from the tau R2 and R3 domains. Several N-amino peptides (NAPs) inhibit tau fibril formation in vitro. We further demonstrate that NAPs 12 and 13 are effective at blocking the cellular seeding of endogenous tau by interacting with monomeric or fibrillar forms of extracellular tau. Peptidomimetic 12 is serum stable, non-toxic to neuronal cells, and selectivity inhibits the fibrilization of tau over Aβ.sub.42. Structural analysis of our lead NAPs shows considerable conformational constraint imposed by the N-amino groups. The described backbone N-amination approach provides a rational basis for the mimicry of other aggregation-prone peptides that drive pathogenic protein assembly.