370 results about "Protein aggregation" patented technology

The present invention provides improved methods for the reduction or removal of protein impurities from a complex cellular Streptococcus pneumoniae lysate or centrate comprising serotype 3 polysaccharides involving steps relating to post-lysis heating or pH adjustment. In certain methods, the lysate is heated for a time and at a temperature sufficient to denature proteins present in the lysate and cause their aggregation and precipitation. In one embodiment, the lysate is heated to at least 60° C. for at least 30 minutes to cause protein aggregation and precipitation, more particularly about 60° C. to about 70° C. for about 30 to about 50 minutes, and even more particularly about 65° C. for about 40 minutes. In other methods, the pH of the lysate or centrate is increased to at least 8.0 to improve filterability, more particularly about 8.0 to 8.4, and even more particularly about 8.2. In further methods, heating and pH adjustment steps are combined to cause the aggregation and precipitation of proteins as well as to improve filterability of the lysates or centrates. In other methods, the pH of the lysate or centrate is lowered to about 3.0 to about 5.0 to cause protein aggregation and precipitation. Such methods allow for the production of substantially purified serotype 3 polysaccharide-containing lysates or centrates.

Disclosed are methods of preventing, treating, or diagnosing in a subject a disorder in protein folding or aggregation, or amyloid formation, deposition, accumulation, or persistence consisting of administering to said subject a pharmaceutically effective amount of inositol stereoisomers, enantiomers or derivatives thereof.

The present inventors discovered that incorporating an Fc region and an antigen-binding domain whose antigen-binding activity varies depending on ion concentration into an antigen-binding molecule that binds to an aggregate-forming antigen produces an antigen-binding molecule that can preferentially clear protein aggregates in comparison to protein monomers from plasma. Use of antigen-binding molecules of the present invention allows various diseases stemming from target tissues to be treated target-tissue-specifically. Use of antigen-binding molecules of the present invention enables treatment of diseases caused by protein aggregates.

Compositions useful for treating neurological disorders including neurodegenerative disorders associated with deleterious protein aggregation, aberrant protein folding, such as brain amylogenic diseases, and/or neurodegenerative autoimmune disorders are described. Methods of using said compositions also are described. In particular, methods to treat a neurodegenerative disorder such as Alzheimer's disease and a neurodegenerative autoimmune disorder such as Multiple Sclerosis are contemplated utilizing proteosomes and/or Glatiramer Acetate, wherein the GA is in a submicron emulsion or a nanoemulsion.

A novel treatment of Alzheimer's disease and other disorders involving protein misfolding or aggregation is provided by enhancing or sustaining an antibody response against predominantly directed against pathological protein aggregates or neo-epitopes present on pathogenic forms of said protein or protein complex. Furthermore, therapeutic methods are also described, wherein ex vivo stimulated antigen-selected peripheral blood lymphocytes are regrafted into the cognate donor.

It is intended to provide a food or a drink with a favorable flavor which has an acidic nature, contains protein and minerals, and has been stabilized in dispersion without showing any protein aggregation or the like even in the absence of a stabilizer. It is also intended to provide such an acidic protein food or drink which shows no protein aggregation even in the case of using not only minerals hardly soluble in aqueous media but also highly soluble minerals. By using an acid-soluble soybean protein, it is possible to provide an acidic mineral-containing food or drink which has a high stability without resort to a stabilizer as an essential component. Owing to the acidic nature, moreover, a product having a refreshing flavor, which is never achieved by neutral foods or drinks, can be prepared.

The invention discloses a method for monitoring beta amyloid protein aggregation process by aggregation-induced emission, belonging to the technical field of biomedical research and clinical detection. With the method, the high affinity between sulfydryl on cysteine and maleimide is utilized to specially combine the beta amyloid protein on an aggregation-induced emission probe. The beta amyloid protein aggregation process is monitored on the basis of aggregation-induced emission enhancement phenomenon. The method has the advantages of high sensitivity, high selectivity, good stability, low manufacture cost and the like and is easy to control. The A beta42 and A beta40 contents can be monitored in a micromole, even a nano-mole level, the detection speed of the method is improved by 15 times if being compared with that of the detection method which utilizes probes, such as ANS (8-aniline-1-naphthalene sulfonic acid) and the like. The beta amyloid protein aggregation process can be qualitatively and quantitatively monitored, the method has a good application prospect if being applied to the pathologic diagnosis of latent patients suffering from senile dementia.

The invention provides compositions, methods and uses comprising a scyllo-inositol compound that provide beneficial effects in the treatment of a disorder and/or disease including a disorder in protein folding and/or aggregation, and/or amyloid formation, deposition, accumulation, or persistence.

The present invention relates to processes for the removal of unwanted protein aggregates from antibody preparations. One process involves removal when the aggregate and antibody are very close in pI value (“Bind-Elute” process). Another process involves the removal when the aggregate and antibody are very close in net electric charge and retention time on ion exchange resin (“Bind-Washout” process). Using either process, at least 90% of the antibody is recovered and 70-90% of the aggregate is removed.

This invention is a method of using a class of excipients for protein formulation to reduce and/or eliminate protein aggregation in solutions or solids. This class of compounds contains carbonyl group(s) to form Schiff base(s) with amino groups of proteins and also contains moieties to keep protein molecules spatially separated. This method has never been disclosed anywhere in the literature.

The present invention relates to methods and assays for identifying agents capable of inhibiting the mutant huntingtin protein, inhibiting or reducing cell death, in particular cell death associated with polyglutamine-induced protein aggregation, which inhibition is useful in the prevention, amelioration and/or treatment of neurodegenerative diseases, and Huntington's disease more generally. In particular, the present invention provides methods and assays for identifying agents for use in the prevention and/or treatment of Huntingtons disease. The invention provides polypeptide and nucleic acid TARGETs and siRNA sequences based on these TARGETS.

The invention relates to self assembling beta-strand peptides for forming nanostructures, compositions containing the peptides, and methods of forming the peptides. The invention further relates to uses of these peptides in drug delivery and enhancement of drug solubility, biomolecule detection, and biocatalysis applications. The peptides of this invention are further useful in models of protein aggregation disease.

The invention discloses human papillomavirus (HPV) antigen formulations which prevent protein aggregation and show prolonged stability as aqueous solutions. These formulations comprise a salt (such as sodium chloride) and a non ionic surfactant (Polysorbate 80 such as Tween 803) in physiologically acceptable concentrations.

The invention discloses an application of a guanidino compound represented by formula I or a pharmaceutically acceptable salt of the guanidino compound in the preparation of medicines for treating nervous system degenerative diseases. R in the formula I is hydrogen, a carboxyl group or a -C1~C5 alkyl-carboxyl group. The guanidino compound has a substantial protection effect on hydrogen peroxide induced neonatal rat hippocampal nerve cell injures, has a substantial inhibition effect on in vitro beta-amyloid protein aggregation, and has potential clinic application values.

A method for making a milk protein concentrate can comprise heating a liquid milk composition at near its natural pH to a temperature that causes the whey protein in the milk to bind to the casein in the milk to form protein aggregates. After cooling, the liquid milk composition can be subjected to membrane filtration using a membrane filter having a large pore size. The protein aggregates are retained to yield a milk protein concentrate. The concentrate can be further treated to provide a concentrate having a lowered lactose content.

Polynucleotide molecules and the proteins encoded by the molecules, diagnostic and treatment methods for neurological disorders characterized by protein aggregation are provided. Genes are described herein that affect the misfolding of, and subsequent aggregation of, aggregation-prone proteins such as alpha-synuclein and have implications for the diagnosis and treatment of neurological diseases related to protein aggregation such as Parkinson's disease. Knockdown of expression of the genes described herein using RNAi results in alpha-synuclein protein aggregation in a C. elegans model of protein aggregation. Dopaminergic neuroprotection after exposure to the neurotoxin 6-OHDA or overexpression of alpha-synuclein may also be provided by overexpression of proteins. Knowledge of genes relating to protein misfolding and aggregation provides powerful means to develop diagnostic screening methods, mutation analysis and drug design information for the development of novel therapeutic and neuroprotective compounds to treat neurodegenerative diseases such as Parkinson's disease.

Process for preparing a purified immunoglobulin preparation. The process comprises the steps of subjecting a crude immunoglobulin solution to caprylic acid treatment, removing protein aggregates and viruses from the immunoglobulin solution, subjecting the immunoglobulin solution to anion exchange chromatography in order to purify the immunoglobulin, filtering the immunoglobulin solution thus obtained on a virus-removal filter to produce an eluate containing immunoglobulin, and recovering the immunoglobulin. By combining caprylic acid treatment and precipitation with a protein precipitant the level of aggregated proteins and viruses is effectively reduced and a truly virus safe preparation is provided after filtration.

The present invention generally relates to engineered bacteriophages which express amyloid peptides for the modulation (e.g. increase or decrease) of protein aggregates and amyloid formation. In some embodiments, the engineered bacteriophages express anti-amyloid peptides for inhibiting protein aggregation and amyloid formation, which can be useful in the treatment and prevention of and bacterial infections and biofilms. In some embodiments, the engineered bacteriophages express amyloid peptides for promoting amyloid formation, which are useful for increasing amyloid formation such as promoting bacterial biofilms. Other aspects relate to methods to inhibit bacteria biofilms, and methods for the treatment of amyloid related disorders, e.g., Alzheimer's disease using an anti-amyloid peptide engineered bacteriophages. Other aspects of the invention relate to engineered bacteriophages to express the amyloid peptides on the bacteriophage surface and/or secrete the amyloid peptides, e.g., anti-amyloid peptides and pro-amyloid peptides, and uses thereof for modulation protein aggregates and amyloid formation.