125 results about "Protein aggregation" patented technology

Provided herein are certain compounds and imaging agents useful for detecting a disease or condition associated with protein aggregation, compositions thereof, and methods of their use.

The invention provides a preparation method and application of a compound protein preparation, and the preparation method comprises the following steps: dissolving a protein matrix in deionized water, adjusting the pH value to 8.0-8.5, firstly adding an antioxidant, and then adding an oxidant and a reducing agent to obtain a protein coupling solution; dissolving the whey protein isolate in deionized water, adding a thickening agent, stirring, and cooling to room temperature to obtain a proteoglycan composite water phase; and mixing the protein coupling solution and the proteoglycan composite water phase according to a preset proportion, adding the oil phase, carrying out homogenization treatment to form a high internal phase emulsion, carrying out freeze drying, and crushing into particles to obtain the powdery protein pre-preparation. The structural stability of protein molecules is remarkably improved, and protein aggregation and sedimentation are reduced, so that the physical and chemical stability of the protein preparation in the storage and use processes is effectively improved, and the problem of insufficient structural stability in the prior art is solved.

Disclosed is a novel class of fusion proteins to recruit the cell's innate chaperone machinery, specifically the Hsp70-mediated system, to specifically reduce TDP-43-mediated protein aggregation and associated protein conformational diseases.

The present invention relates to a low fat milk cream product wherein the product is an emulsion having: (a) between 1% and 5% by weight, preferably between 2% and 4% by weight of milk protein; (b) between 5% and 20% by weight, preferably between 10% and 18% by weight of fat; (c) between 0.002 wt% and 0.3 wt% of a mineral salt, such as between 0.03 wt% and 0.3 wt% of sodium chloride and / or between 0.002 wt% and 0.02 wt% of calcium chloride; (d) optionally between 0.1% and 3% by weight of a food additive, preferably a hydrophilic colloid, and (e) between 70% and 90% by weight of water; wherein the milk protein is contributed by (i) skimmed milk powder or milk protein concentrate or micellar casein.

The invention discloses a high-emulsification-activity gluten protein based on irradiation modification and a preparation method thereof in the field of wheat protein processing, and the method comprises the following steps: dispersing wheat gluten protein in deionized water, stirring to form a uniform suspension, adjusting the pH value, carrying out enzymolysis treatment on the suspension by using alkaline protease, and drying to obtain the high-emulsification-activity gluten protein. Centrifugally drying to obtain primary protein powder; dissolving the protein primary powder in an irradiation solvent to obtain a protein dispersion liquid, and irradiating the protein dispersion liquid by using cobalt-60 gamma rays as an irradiation source in an intermittent manner; and taking the irradiated protein dispersion liquid, and performing centrifugal drying to obtain the high-emulsification active gluten protein. The method comprises the following steps: firstly, carrying out limited hydrolysis on gluten protein by using protease to generate a smaller peptide fragment, so that the irradiation efficiency and the emulsion stability are improved; by adopting an intermittent irradiation treatment mode, protein aggregation caused by heat effect can be reduced, the emulsifying effect is improved, and the stability and adhesive force of an adhesive can be improved when the emulsion is applied to the adhesive.

Disclosed herein are multifunctional polypeptides comprising an optional signal peptide sequence, a cell penetrating peptide, an antigen binding domain (e.g., anti-synuclein, anti-tau, anti-huntingtin), and a programmable proteasome-targeting PEST motif, and methods for using these polypeptides in treatment of protein aggregation diseases, e.g., neurodegenerative diseases.

The present disclosure relates generally to compositions, systems, and methods for lysing blood samples comprising an infectious agent, for example a bacteria, or a fungus, while maintaining viability of the infectious agent for subsequent characterization, for example phenotyping or genotyping. A lysing composition may include one or more surfactants, such as one or more detergents. A lysing composition may include lysing agent including one or more salts. A lysing composition may include one or more enzymes to break down one or more lyses byproducts, such as nucleic acids and / or protein aggregates.

Provided herein is a method of decreasing a-syn levels and / or decreasing a-syn toxicity in a cell, the method comprising contacting the cell with a charged multivesicular body protein 2B: a-synuclein (CHMP2B:a-syn) inhibitor and a method of inhibiting neural degeneration, the method comprising administering to a subject in need thereof a charged multivesicular body protein 2B: a-synuclein (CHMP2B:a-syn) inhibitor.

Compounds comprising an amide-linked coumarin scaffold, compositions comprising same, and method of using such compounds and compositions to inhibit tubulin-associated unit (tau) protein aggregation or alpha-synuclein ( α-syn) protein aggregation in a subject having, or at risk for, tau protein aggregation or α-syn protein aggregation, respectively.

The invention relates to methods and materials for use in treating neurodegenerative diseases associated with pathological protein aggregates and provides fusion proteins comprising: (i) a first portion comprising a sequence of a protein which aggregates pathologically in neurodegenerative disease, such as tau protein, and (ii) a second portion comprising a RING-type E3 ubiquitin ligase, a component of a RING-type E3 ubiquitin ligase complex, or a domain of either. These fusion proteins have utility in selectively or preferentially targeting pathogenic protein aggregates for degradation.

The present application provides methods, compositions and kits for determining SHD-catalyzed antibody levels in a biological sample and for treating or preventing protein aggregation disease (PAD) in an individual. Catalytic antibodies that specifically recognize amyloid beta (A beta) peptides and methods of using the same are also provided.

The technical problem of the present disclosure is to provide: a composition for promoting the decomposition of protein aggregates; and a pharmaceutical composition for preventing or treating neurodegenerative diseases associated with the formation of protein aggregates. The technical problem is solved by a compound represented by general formula (I).

The invention discloses a method for sterilizing a vegetable protein beverage, which comprises the following steps of: adding a composite antibacterial microsphere preparation into a vegetable protein beverage to be treated, uniformly mixing, and performing high-density CO2 treatment and magnetic induction electric field sterilization to obtain a vegetable protein beverage finished product, the composite antibacterial microsphere preparation is prepared by taking fucoidan and a gallic acid acylated quercetin-phospholipid conjugate as a substrate and loading lysozyme and hydroxytyrosol. High-density CO2 and a magnetic induction electric field are adopted for synergistic sterilization, so that the structure of a microbial film can be changed, metabolism is disturbed, a good matrix is provided for electric field sterilization, and the sterilization efficiency is further improved through electric breakdown, magnetic field refining of water molecular groups and heat effect; the composite microspheres are sensitive to an electric field, so that lysozyme and hydroxytyrosol can be triggered to be accurately and quickly released under the action of a magnetic induction electric field, stubborn spores can be efficiently killed, and the killing effect is improved by destroying cell wall structures and disulfide bonds of the spores; meanwhile, protein aggregation and flocculation in the beverage can be effectively prevented, and the stability of a beverage system is guaranteed.

The application relates to the medical technology field and discloses an oral liquid capable of easily expelling stones and clearing toxins and a preparation process thereof. The raw materials of the oral liquid include chicken gizzard suet, dandelion, houttuynia cordata, sea golden sand, plantain, corn silk, money grass, corydalis, licorice and oligofructose with a specific polymerization degree. The preparation process comprises grouping extraction of the raw materials, purification of the chicken gizzard suet by using concentration with forced circulation and bottom feeding type jet flow, pressure filtration of the sea golden sand by using the endogenous fiber of the houttuynia cordata to construct a filter aid skeleton, and finally constant-temperature liquid preparation and sterilization by using a micropore filter membrane to obtain the finished product. Oligofructose is introduced into traditional Chinese medicine to promote proliferation of intestinal oxalic acid degrading bacteria, and plant components are used to block stone generation from a metabolic source; specific fluid mechanics separation and non-thermal sterilization processes solve the problems of protein aggregation and micropore blockage of microspores, and the configuration stability of heat-sensitive medicinal components and prebiotic molecules is maintained.

The application provides a screening device and method and application of small molecules for inducing or inhibiting protein polymerization, adopts a solid-state quartz nanopore as a core detection device, drives target proteins or complexes of the target proteins and small molecules to pass through a nanoscale pore, records ion current changes caused by each time of perforation event in real time, analyzes peak current and residence time characteristic values of each event, and can identify whether the proteins are in monomer, oligomer, aggregation or LLPS state. Meanwhile, the nanopore sensing is combined with small molecule processing, a mapping relationship between current signal changes and aggregation state regulation is established, and screening of small molecules for inducing or destroying protein aggregation behavior is realized. The technology has multiple advantages of label-free, single molecule, real-time monitoring and adaptation to multiple protein aggregation states, and breaks through the bottleneck of throughput and resolution capacity of existing methods.

Disclosed herein are small molecule drugs that reduce protein aggregation and their methods of use. One aspect of the invention provides for a method reducing aggregate protein abundance in a protein aggregate, the method comprising administering an effective amount of a compound that stably binds a Glial Fibrillary Acidic Protein (GFAP) to a subject, wherein the aggregate protein comprises BSN, SYN1, MAP2, PLEC, RAB10, MAP1A, DCTN, TUBA4A, SPARE, PRKDC, or any combination thereof.

The invention relates to a wet spinning preparation process of protein modified polyacrylonitrile fibers, and relates to the field of wet spinning preparation processes, the wet spinning preparation process comprises the following steps: S1, heating and softening a spinning stock solution, dropwise adding a protein solution, and fully dissolving to obtain a clear and transparent protein modified spinning solution; s2, the protein modified spinning solution is sequentially subjected to filtering, defoaming, spinning, coagulating bath and drafting, and then the protein modified polyacrylonitrile fiber is obtained; the spinning stock solution is an acrylonitrile-methyl acrylate-itaconic acid ternary copolymerized stock solution. The acrylonitrile-methyl acrylate-itaconic acid ternary copolymerized stock solution is adopted as a spinning matrix, the compatibility with natural protein is improved by introducing a polar group, and the protein is uniformly dispersed at a molecular level in cooperation with a mode of dropwise adding the protein solution after heating and softening, so that the protein agglomeration phenomenon is remarkably reduced, and the uniformity of the internal structure of the fiber is improved.

The invention relates to a method of detecting cancer in a subject based on the level of p53 protein aggregates in a body fluid sample from the subject. The invention also relates to corresponding methods of determining the risk of cancer in a subject, monitoring the progression or onset of cancer, and / or determining the efficacy of a therapeutic intervention for treating cancer in a subject. The invention further relates to kits for use said methods.

The present invention is directed to stabilized protein-containing formulations, stabilized or inhibited against protein aggregation, comprising an amphiphilic surfactant.

The invention discloses a sequential enzymatic-ionic synergistic soybean protein isolate modification method, which comprises the following steps: dispersing soybean protein isolate in water to prepare a protein solution, adding glutamine transaminase, carrying out heating reaction to inactivate enzyme to obtain an enzyme cross-linked protein solution, adding MgCl2 into the enzyme cross-linked protein solution, and carrying out heating reaction to induce protein aggregation to obtain a modified soybean protein isolate solution; and cooling to room temperature after the reaction is finished. The invention also discloses an application of the soybean protein product obtained by the sequential enzymatic-ionic synergistic soybean protein isolate modification method as a food additive. According to the method, the sensitization of the soybean protein can be remarkably reduced, meanwhile, the unique stomach resistance-intestinal efficient release dynamic characteristic is shown, and the small intestine peptide fragment release amount is promoted to be increased.

The invention belongs to the field of small molecule polypeptides, and particularly relates to a scallop polypeptide with a protein aggregation resisting function and application of the scallop polypeptide. The pure natural scallop polypeptide is extracted, separated and identified by taking scallops as raw materials through the steps of enzymolysis separation, ultrafiltration purification, LC-MS / MS identification and the like, the amino acid sequence of the scallop polypeptide is TMYWTDVSNGQIHR, the molecular formula is C74H110N22O23S, the average relative molecular mass is about 1707.88 Da, the theoretical isoelectric point is pH = 6.41, and the scallop polypeptide is hydrophilic polypeptide. The scallop polypeptide has the functions of oxidation resistance, protein aggregation resistance and neuroprotection, can be further applied to development of products such as food, medicines and health care products, and has a wide application prospect.

The present disclosure describes, compositions and methods comprising a recombinant, chimeric poliovirus construct for the neuroinflammatory stimulation of microglia against neurodegenerative diseases. The compositions may include a chimeric poliovirus and a therapeutic agent capable of binding to protein aggregates associated with the neurodegenerative disease. Methods of treating neurodegenerative diseases and methods of activating microglia are also provided.

To provide technology that can be used to inhibit aggregation of β-amyloid protein (Aβ) and microtubule-binding protein Tau, which bring about senile plaque (senile plaque: AP) and neurofibrillary tangle (Neurofibrillary Tangle: NFT).SOLUTION: The present invention provides a protein aggregation inhibitor containing mesostructured particles of calcium hydrogen carbonate as an active ingredient.SELECTED DRAWING: Figure 2

The embodiment of the invention discloses a composite freeze-drying protective agent based on CRISPR-Cas13a, a microsphere molecular diagnostic reagent and a preparation method. The composite freeze-drying protective agent comprises a vitrification matrix component, a structure support component, a protein aggregation inhibitor and a surfactant, the vitrification matrix component comprises mannitol and trehalose, and the mass ratio of mannitol to trehalose is (3-7): (3-7); the structural support component comprises any one of PEG8000, PEG6000 and PEG4000 and any one of glucan 10000, glucan 8000 and glucan 20000, and the mass ratio of the PEG8000 to the PEG6000 to the glucan 8000 to the glucan 20000 is (1-5): (1-5); the protein aggregation inhibitor is bovine serum albumin, and the surfactant is polyoxyethylene sorbitan monolaurate; the mass ratio of the structure supporting component to the vitrification matrix component is (1-5): (3-7), the mass ratio of the protein inhibitor to the structure supporting component is (0.01-1): (2-10), and the mass ratio of the surfactant to the structure supporting component is (0.001-0.1): (2-10).

The present invention relates to a method and system (140) for determining the presence and / or quantity of protein aggregates in a liquid sample comprising a protein. The method comprises: a) measuring ultraviolet-visible spectroscopy (UV- Vis) absorbance of the sample to obtain a UV-Vis absorbance measurement; b) measuring index of refraction (IoR) of the sample to obtain an IoR measurement; c) determining a value for the UV-Vis absorbance measurement; d) determining a value for the IoR measurement; and e) determining the presence and / or quantity of protein aggregates in the sample based on a ratio between the value for the UV-Vis absorbance measurement and the value for the IoR measurement.

A number of protein aggregation diseases are associated with accumulation of misfolded proteins, which are known as protein aggregates, including, but not limited to, neurodegenerative and non-degenerative diseases and disorders. The present disclosure provides an assay, compositions and kits for the qualitative and quantitative assessment of aggregated proteins in solution using a microparticle immunocapture assay that combines the advantages inherent to a specific first and second capture moiety that binds specifically to an aggregated protein which can reveal at the same time the amount and the size of aggregates measured in a sample, fluid, tissue, cavity, or pharmacological product.

The invention discloses a silk fibroin solution desalination and concentration system based on multi-stage membrane separation coordinated regulation, which breaks through the limitation of the traditional single membrane separation technology through integrated optimization of a microfiltration-washing filtration desalination-concentration three-stage membrane separation process, and realizes step-by-step precise treatment of a silk fibroin solution. In the microfiltration stage, macromolecular impurities are removed through synergism of dilution and pre-filtration, and a stable raw material is provided for subsequent precise separation; dynamic filter washing and membrane screening effects are combined in the filter washing and desalting stage, so that the desalting efficiency is remarkably improved; in the concentration stage, through membrane interception and volume regulation and control, the target concentration is realized while the salinity is reduced, protein aggregation is avoided, and stable product quality is ensured. Through multi-dimensional linkage of the conductivity sensor, the liquid level sensor and the pH sensor, automatic closed-loop control over the desalination degree, the concentration end point and wastewater discharge is achieved. The dynamic filter washing and secondary purification trigger mechanism ensures the consistency between batches, and the purity of the final product and the process stability are remarkably improved.

The invention discloses a technology for removing viruses from tetanus human immune globulin through a nano film. The process comprises the following steps: pretreating a feed liquid, so that the protein concentration of the feed liquid is 50-60g / L, the pH is 3.8-4.4, and the feed liquid contains 90-110g / L maltose and 50-150mmol / L sodium chloride; then, the feed liquid is subjected to two-stage filtration through a 0.1-micron nylon pre-filtration membrane bag with negative charges and a 20-nm regenerated cellulose (RC) virus removal membrane bag in sequence. According to the process, through optimizing the physical and chemical state of the feed liquid and the synergistic effect of the feed liquid and the functionalized filter membrane, the protein aggregation is effectively inhibited, the membrane pollution is reduced, the virus removal effect is ensured not to be lower than 4log10, the protein load of the RC membrane is remarkably improved to be more than 200L / m, and the product purity is more than or equal to 98%. The invention solves the technical problems of low flux and easy blockage of high-concentration immune globulin in small-aperture virus removal filtration, and is suitable for efficient, safe and large-scale production of blood products.

Novel materials and methods are provided for treating neurodegenerative diseases associated with protein aggregates by selectively targeting the aggregates. The present invention relates to methods and materials for use in treating neurodegenerative diseases associated with pathological protein aggregates, and provides fusion proteins comprising (i) a first portion comprising the sequence of a protein that pathologically aggregates in neurodegenerative diseases, such as tau protein, and (ii) a second portion comprising a RING-type E3 ubiquitin ligase, a component of a RING-type E3 ubiquitin ligase complex, or a domain of either. These fusion proteins are useful for selectively or preferentially targeting pathogenic protein aggregates for degradation.

The present invention is directed to a protein aggregation assay, and methods of use thereof.