181 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 bispecific antibody and a purification method thereof. The purification method comprises the following steps: a) loading a sample containing a bispecific antibody to a affinity chromatographic column, and leaching and eluting; the biomacromolecules in the sample are adsorbed on the affinity chromatography column in the leaching stage, the biomacromolecules comprise antibodies, host cell proteins and protein aggregates, and the antibodies comprise bispecific antibodies and homodimers; separating the antibody from the affinity chromatography column in the elution stage, and collecting the eluate in the elution stage; b) loading the eluent to a hydrophobic membrane material, carrying out flow-through, and collecting a flow-through liquid containing the purified antibody; and the flow-through liquid used for flow-through contains 0.73 to 0.77 M of (NH4) 2SO4. The method can solve the problem that homodimers in bispecific antibodies are difficult to efficiently remove in the prior art, and is suitable for the field of antibody purification.

The invention discloses a fusion antibacterial peptide BMAP18-BSN37 and application thereof, and belongs to the technical field of gene engineering. The nucleotide sequence of the fusion antibacterial peptide BMAP18-BSN37 is as shown in SEQ ID NO. 1, and the amino acid sequence of the fusion antibacterial peptide BMAP18-BSN37 is as shown in SEQ ID NO. 2. The fusion antibacterial peptide BMAP18-BSN37 gene is inserted into a pNZ8148 expression vector to construct a recombinant expression vector pUBB, so that protein aggregation or degradation in cells can be avoided, and the survival rate of strains and the stability of protein expression are improved. The method comprises the following steps: transferring a plasmid pUBB into a lactic acid bacteria NZ9000 strain through electrotransformation, and screening a recombinant lactic acid bacteria strain capable of expressing a fusion protein BMAP18-BSN37 to obtain a recombinant strain NZ-BB; the recombinant lactic acid bacteria NZ-BB strain shows a remarkable prevention effect in an animal infection model, and can effectively reduce bacterial colonization and relieve pathological injury; the Salmonella strain has the potential of being used as an animal feed additive, can reduce the use of antibiotics and chemicals, slow down the development of bacterial drug resistance, improve animal immunity and slow down intestinal inflammation caused by salmonella, and provides support for effectively preventing the health of livestock and poultry.

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.

The present disclosure provides anti-amyloid [beta] (A [beta]) antibodies and antibody fragments that preferentially bind to soluble amyloid [beta] fibrils / oligomers and trigger ADPC in microglial cells; anti-amyloid [beta] (A [beta]) antibodies and antibody fragments that reduce soluble amyloid [beta] fibril / oligomer levels and insoluble amyloid [beta] plaques in brain tissue; and the use of anti-A [beta] fibril / oligomer antibodies and antibody fragments in the treatment, prevention, diagnosis, screening and monitoring of conditions associated with A [beta] protein aggregation, in particular Alzheimer's Disease (AD).

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 invention relates to a formulation of an Engrail (EN) protein, and more particularly to an aqueous formulation of an Engrail (EN) protein capable of inhibiting or minimizing aggregation of the EN protein. In some embodiments, the formulations of the present invention are capable of inhibiting or minimizing dimerization and / or oligomerization of an EN protein, which is a monomer.

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 phospholipid compound for inhibiting beta-amyloid protein aggregation, and the chemical structural formula of the phospholipid compound is as follows: # imgabs0 #, and n is an integer greater than 2. Dioleoyl phosphatidyl ethanolamine molecules are modified by utilizing maleimide alkyl carboxylic acid and glutathione, so that the interaction between a phospholipid compound and amyloid protein can be effectively regulated and controlled, and the aggregation of the amyloid protein is delayed and even inhibited; the preparation method is simple, the reaction energy consumption is low, and the obtained phospholipid compound has good biocompatibility and is suitable for popularization and application.

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.

To provide a pharmaceutical formulation comprising trehalose for use in treating myopathies, neurodegenerative diseases, or tauopathies associated with abnormal protein aggregation.SOLUTION: A pharmaceutical formulation comprising a therapeutically effective amount of trehalose is provided, wherein the pharmaceutical formulation is for use in a method for treating a disease associated with abnormal protein aggregation and / or inclusion bodies formation in myocytes, neurons, or extracellular compartments, or for alleviating at least one symptom associated therewith in a human subject in need thereof, the method comprising intravenously administering to the subject a pharmaceutical formulation comprising 0.1% (w / v) to 50% (w / v) of trehalose. An injectable aqueous pharmaceutical formulation comprising a therapeutically effective amount of trehalose is also provided.SELECTED DRAWING: None

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 invention relates to the technical field of preparation and application of bioindustry peptides and immune globulins, in particular to a preparation method of human immune globulins stored at normal temperature. The preparation method comprises the following steps: treating an FI + II + III / FII + III precipitation dissolving solution by using fumed silica Aerosil380, and adsorbing and removing unstable substances such as lipoprotein and lipoid in the precipitation dissolving solution so as to reduce protein polymerization caused by the unstable substances in a long-term normal-temperature storage process, so that the long-term stability of the human immune globulin is improved; l-proline is added into the final formula of the product to reduce the polymerization and oxidation effects of protein in the storage process, trace Tween 80 is added into the final formula of the product to reduce the viscosity of the protein, and the operation conditions of adding the L-proline through ultrafiltration and concentration are further optimized to further prevent or reduce the polymerization of the protein so as to realize normal-temperature storage of the human immune globulin.

The invention relates to the field of biology, in particular to a duck TRPA1 protein extra-membrane part polyclonal antibody as well as a preparation method and application of the duck TRPA1 protein extra-membrane part polyclonal antibody. The invention provides a duck TRPA1 protein out-of-membrane part polyclonal antibody prepared from TRPA1 recombinant protein and a preparation method of the duck TRPA1 protein out-of-membrane part polyclonal antibody, the titer of the duck TRPA1 protein out-of-membrane part polyclonal antibody is greater than or equal to 1: 256000, and the duck TRPA1 protein out-of-membrane part polyclonal antibody is strong in specificity. The TRPA1 extracellular region (103bp-1051bp) is accurately selected through bioinformatics analysis, so that the expression difficulty caused by a hydrophobic structure of a transmembrane region is avoided, and the target functional epitope of the antibody is ensured; protein aggregation is reduced by utilizing stepped renaturation, and a high-purity antigen is obtained by matching with molecular sieve chromatography; an antigen is coupled with an NHS-active HP column, specific IgG is efficiently captured through a one-step method, and serum impure protein is removed.

The invention provided herein relates to methods for measuring protein aggregation and stability. The method can be used for characterizing cell-free protein synthesis reactions.