61 results about "Amyloid fibril" patented technology

The invention relates to the technical field of hydrogel, in particular to a preparation method and application of EGCG-mediated hydrogel, a lysozyme solution is heated under the acidic condition to form lysozyme amyloid fibrils LAFs, EGCG is dissolved in a buffer solution and mixed with the LAFs solution obtained in the step 1 in proportion to form an LAFs-EGCG compound, and the EGCG-mediated hydrogel is prepared. The chitosan CS is dissolved in an acetic acid buffer solution, glutaraldehyde is added to serve as a cross-linking agent, the mixture is mixed with the LAFs-EGCG compound obtained in the step 2 and stirred, the composite hydrogel is formed, the concentration of EGCG is 0.2-1.0 wt%, the concentration of LAFs is 5 wt%, the concentration of chitosan is 2 wt%, the pH value of the lysozyme solution in the step 1 is 2.0, the heating temperature is 77 DEG C, the heating time is 10 hours, the concentration of EGCG in the step 2 is 0.4-0.8 wt%, and the pH value of the lysozyme solution in the step 2 is 1.5-2.5. In the step 3, the concentration of glutaraldehyde is 2%, the storage modulus G'of the hydrogel is 325-480 Pa, the hardness is 2176.71 g, and the bacteriostasis rate on staphylococcus aureus and salmonella exceeds 95%.

The invention relates to an isolated monoclonal antibody or antigen binding portion thereof which specifically binds to amyloid fibrils and effectively promotes clearance of extracellular amyloid deposits from the tissues in vivo, as well as humanised antibodies having the same properties.

The present invention concerns the use of peptidyl-prolyl isomerase cyclophilin 40 (CyP40) for reduction of neurotoxic fibrils and treatment and prevention of neurodegenerative diseases associated with amyloid fibril aggregation. Aspects of the invention include compositions, methods, dosage forms, and kits for treating or preventing a neurodegenerative disease or condition associated with amyloid fibril aggregation in a human or animal subject, and for disaggregating neurofibrillary aggregates in vitro or in vivo, using CyP40, or a biologically active fragment thereof.

The invention discloses a preparation method of an interface evaporator with an amphiphilic micro-nano structure, wherein graphene oxide sheets are weighed and dispersed in an acidic aqueous solution to obtain a graphene oxide dispersion, the graphene oxide dispersion is then added to an amyloid fibril solution for stirring, and then a hydrazine hydrate solution is added for reduction reaction to obtain a SPI-AFs@rGO pre-gel solution of soybean protein isolate amyloid fibrils combined with reduced graphene oxide; thereafter, glutaraldehyde is added for further cross-linking to obtain a SPI-AFs@rGO-Gel hydrogel. The method of the invention utilizes the electrostatic adsorption of reduced graphene oxide and amyloid fibrils under acidic conditions to construct a soybean protein isolate amyloid fibril-based aerogel with a porous structure, and at the same time regulates the hydrophilicity of the amyloid fibrils at a micro-nano scale to improve the evaporation rate of the photothermal interface evaporator.

The invention provides a pH response type composite hydrogel dressing as well as a preparation method and application thereof, and belongs to the technical field of medical materials. According to the pH response type composite hydrogel dressing, gel formed by crosslinking glycyrrhetinic acid and ovalbumin amyloid fibrils is used as a carrier, and a zinc ion modified metal organic framework material is loaded on the carrier. Functional groups such as carboxyl and hydroxyl of glycyrrhetinic acid are combined with ovalbumin amyloid fibrils through hydrogen bonds and electrostatic interaction to form a hydrogel carrier, and then a zinc ion modified metal organic framework material is loaded on the hydrogel carrier to obtain the composite hydrogel dressing. The hydrogel has antibacterial and anti-biofilm effects on escherichia coli and staphylococcus aureus, has good biocompatibility and mechanical properties, has pH responsiveness, and can realize programmed control to actively remove bacteria.

The use of amyloid fibrils for providing nutritional minerals to the human body, particularly as a component in a food product, a dietary supplement or in a pharmaceutical product. Compositions including composite materials of amyloid fibrils and nutritional minerals. The use of such composite materials in the treatment of diseases and disorders and to the fortification of food and dietary supplements with nutritional minerals.

The present invention relates to a gene therapy for treating synucleinopathies. The present invention provides a novel α-Syn peptide variant and inhibits the formation of amyloid fibrils and degrades α-Syn aggregates, thereby exhibiting excellent preventive, ameliorative, and therapeutic effects on synucleinopathies.

The details of the mechanistic relationships between the pathogenesis of Alzheimer's disease, Aβ production, and tau-mediated neurotoxicity remain poorly understood. There remains the potential for improved therapies that target both Aβ production and tau-containing neurofibrillary tangles. Thus, there is a need for specific and effective therapeutic agents that target Aβ and tau. [Solution] Disclosed herein are antibodies for treating or preventing Alzheimer's disease, including anti-Aβ protofibril antibodies and anti-tau antibodies, pharmaceutical preparations, methods for treating or preventing Alzheimer's disease, and kits including pharmaceutical preparations for treating or preventing Alzheimer's disease.

The invention discloses flexible amyloid fiber gel based on albumin and lysozyme as well as a preparation method and application of the flexible amyloid fiber gel, and belongs to the field of delivery of natural high polymer materials and bioactive substances. The method comprises the following steps: respectively preparing ovalbumin fibers (OVAf) and lysozyme fibers (LYZf), mixing according to a volume ratio of 2: 1, adding resveratrol with a final concentration of 100 [mu] mol / L, and incubating at 37 DEG C for 3 h to form flexible gel; according to the gel, ordered crosslinking of fibers is induced through resveratrol, a uniform three-dimensional network is formed, and the gel has good elasticity and flexibility; when being used as a carrier to embed active ingredients such as anthocyanin, the nano-carrier can significantly improve the storage stability and digestion environment tolerance, and has excellent biocompatibility. The invention provides a new scheme for efficient delivery of bioactive components, and can be applied to the fields of functional foods, biological medicines and the like.

The present invention discloses a method for monitoring the amyloid fibrillization process of lysozyme based on cluster luminescence. The method utilizes the property that lysozyme itself can emit fluorescence in an aggregated state, and the intensity of the fluorescence changes with the change of the aggregation state of lysozyme, thereby achieving the purpose of monitoring the amyloid fibrillization process of lysozyme. The method only needs to perform fluorescence detection on the fluorescence of the protein solution that can form amyloid fiber aggregates, without the introduction of exogenous fluorescent probes. The method is simple and has lower cost. The method can fully present the overall process of amyloid fibrillization and has the advantage of high sensitivity, especially high sensitivity to the early stages of amyloid fibrillization.

Compounds useful for treating or preventing diabetes and related conditions, and for preventing, inhibiting or reversing amylin-amyloid fibril formation, preventing islets of Langerhans (Beta)-cell death, preventing or reversing the transition from soluble human amylin to insoluble human amylin, preventing and inhibiting or reversing cytotoxic amylin fibril formation. The invention relates to compounds of Formula (I): (I)

The invention discloses application of a theaflavin compound in preparation of a medicine for inhibiting beta amyloid peptide aggregation, and belongs to the technical field of biological medicine. Multi-dimensional experiments prove that the galloyl group in the theaflavin compound can significantly inhibit the formation of Abeta42 amyloid fibers, reduce the generation of toxic oligomers and reconstruct formed oligomers by increasing binding sites with Abeta42 polypeptide and enhancing polar interaction and hydrophobic interaction. The TF3 (containing two galloyl groups) has the optimal anti-Abeta 42 polypeptide aggregation activity, a precise target spot is provided for design of an Abeta amyloid aggregation inhibitor taking the galloyl groups as a core structure, and an experimental basis is provided for application of a natural polyphenol compound in preparation of a medicine for preventing or treating Alzheimer's disease.

The application discloses a preparation of a betalain-loaded peanut globulin amyloid fiber / chitosan supramolecular composite coating liquid and application thereof. Firstly, acid heat and ultrasonic treatment are used to induce peanut globulin to form protein amyloid fibers through fiberization, then the peanut globulin amyloid fibers are combined with chitosan to form a complex, and a betalain solution is added, pH is adjusted and stirring is conducted to form the betalain-loaded peanut globulin amyloid fiber / chitosan supramolecular composite coating liquid. The supramolecular composite coating liquid loaded with bioactive substances is prepared through the self-assembly characteristics of the protein amyloid fibers, the process operation is simple, and no organic cross-linking reagent is additionally added in the preparation process, so that the supramolecular composite coating liquid is safe and has no toxic side effects. The supramolecular composite coating liquid prepared by the application can form a fresh-keeping coating on the surface of fruits only through coating treatment, the operation is simple and convenient, the supramolecular composite coating liquid can inhibit the reproduction of bacteria and fungi, is non-toxic, has the effect of prolonging the shelf life of fruits, and is suitable for large-scale production and market promotion.

The invention provides a protein raw material pretreatment method and application, and belongs to the technical field of protein raw material treatment.The protein raw material pretreatment method comprises the steps that a high-fiber protein raw material is prepared and subjected to pulsed electric field PEF treatment, stirring or circulation is conducted in the treatment process to guarantee the treatment uniformity, and after electroporation is generated, the protein raw material subjected to PEF treatment is obtained; the method comprises the following steps: performing PEF treatment on a protein raw material, adjusting the solid-liquid ratio of the protein raw material subjected to PEF treatment, sequentially performing sequential gradient enzymolysis, controlling the peptide chain length by monitoring the enzymolysis degree to obtain a protein hydrolysate with a specific peptide chain length, performing amyloid fibril treatment on the protein hydrolysate, and performing low-temperature drying on the treated product to finally obtain the functional protein raw material. According to the method, the pretreatment uniformity and the enzymolysis efficiency of the protein raw materials can be improved, the peptide chain length is accurately controlled, the protein digestibility is improved, the anti-nutritional factor content is reduced, and the functional protein raw materials suitable for livestock and poultry and aquatic feed production are produced.

The present disclosure relates in some aspects to methods and compositions for reducing or inhibiting amyloid fibril growth.

The present invention provides novel antibodies comprising a Fab region and an Fc region, wherein the Fab region has broad specificity for the different types of amyloid fibrils that cause the major forms of human systemic amyloidosis, and the Fc region is engineered to convey additional advantageous properties such as increasing complement activation, increasing binding to Fcγ receptors and / or increasing half life. The present invention also provides humanised Fc engineered monoclonal antibodies which target multiple amyloid fibril types, as well as methods for using such antibodies and uses of the antibodies in therapeutic applications. The present invention further provides novel antibodies comprising a Fab region, wherein the Fab region has broad specificity for the different types of amyloid fibrils.

Disclosed herein are antibodies, pharmaceutical formulations for treating or preventing Alzheimer's disease, methods of treating or preventing Alzheimer's disease, and kits comprising pharmaceutical formulations for treating or preventing Alzheimer's Disease comprising an anti-Aβ protofibril antibody and anti-tau antibody.

An exemplary system and method are disclosed for a lateral flow immunoassay test designed for testing insulin efficacy and a method of using the device. The exemplary test, and associated device or system, specifically detects ineffective insulin by testing, in an insulin sample, for the presence of amyloid fibrils that may have formed from denatured insulin protein molecules. If amyloid fibrils are present, the antibodies conjugated with a label of the label-conjugated anti-amyloid fibrils (e.g., gold nanoparticles), of the test, would bind to the amyloid fibrils present in the sample to reveal a test line, or other indicator described herein, indicating the presence of amyloid fibrils. The test can employ a secondary antibody as a control line to detect the presence of insulin.

A complex includes an amyloid peptide complexed with a cholinesterase inhibitor, an NMDA receptor antagonist, or a combination, of a cholinesterase inhibitor and an NMDA receptor antagonist, wherein the amyloid peptide comprises X1X2GAIIGX3X4 (SEQ ID NO: 2), wherein X1 and X4 are each independently YF or FY, and X2 and X3 are each 1 amino acid long, and are each independently T, N, S, or Q; or X2 and X3 are each 2 amino acid long and X2 is (Y or F)T, (Y or F)N, (Y or F)S or (Y or F)Q, and X3 is T(Y or F), N(Y or F), S(Y or F) or Q(Y or F), wherein the amyloid peptide self-assembles into amyloid fibrils, and wherein the peptide has a total length of 11-13 amino acids.

Disclosed are agents that include a) a binding and / or disaggregating moiety that adheres to a target polypeptide in its amyloid fibril form, and proceed to inhibit the target protein and / or disaggregate the fibril form, and b) a nanomass moiety that promotes transfer of the agent to a site of the target polypeptide. The disclosed agents can be used in methods for destabilizing a tau amyloid fibril, and for treating a tauopathy (e.g., Alzheimer's disease, progressive supranuclear palsy) in a subject.

Disclosures herein are directed to polypeptide probes that may be used to detect transthyretin (TTR) oligomers or fibrils in patient samples obtained from subjects with wildtype and mutant TTR alleles. Also provided are methods of using the provided probes to diagnose subjects with a TTR-associated disease or condition or for monitoring the efficacy of a therapeutic administered to treat a TTR-associated disease or condition.

The application belongs to the technical field of flavor enhancement materials, and provides a kind of aroma embedding complex based on pea protein amyloid fiber and its preparation method and application.The aroma embedding complex of the application includes pea protein amyloid fiber (PAF), cellulose nanofiber (CNF) and 2,5-dimethylpyrazine.In the aspect of molecular conformation evolution, the orderly arrangement of cross beta-fold structure induced by CNF promotes the further enrichment of hydrophobic sites, forming a "hydrophobic pocket" with more complete structure and better spatial adaptability.Meanwhile, the ordered conformation enhances the hydrogen bond and hydrophobic interaction between PAF and 2,5-dimethylpyrazine molecules, improving the comprehensive affinity of local binding sites.In the aspect of microstructure regulation, the dense network constructed by CNF and PAF cooperatively forms a limited and continuous embedding space, which more effectively constrains aroma molecules in the hydrophobic pocket, further amplifying the overall aroma binding capacity of the system.

The application discloses a HEWL amyloid fiber-chlorogenic acid antibacterial hydrogel and a preparation method and application thereof, and belongs to the technical field of antibacterial hydrogels. In view of the defects of existing hydrogel products, the application provides an antibacterial hydrogel based on chicken egg white lysozyme (HEWL) amyloid fiber and natural polyphenol chlorogenic acid (Chlorogenic acid, CGA) and an application method of the antibacterial hydrogel in fresh beef preservation. The application takes natural food-derived protein amyloid fiber and plant polyphenol as raw materials, forms a three-dimensional gel network structure with good mechanical stability and antibacterial activity through regulation of a self-assembly process, fully plays a synergistic effect of the natural food-derived protein amyloid fiber and the plant polyphenol, and realizes efficient inhibition of gram-positive bacteria and gram-negative bacteria. The preparation process of the application does not need an external crosslinking agent or an organic solvent, the process is simple and has high repeatability, and is suitable for large-scale food-grade production.

This invention provides a method for preparing immobilized lipase using composite-modified protein amyloid protofibrils. The method first prepares β-lactoglobulin amyloid protofibrils by controlling pH and hydrothermal conditions, then polymerizes them into COF protofibrils via TFB and DB condensation. An immobilized carrier is obtained by composite modification with sulfopropyl betaine and pentamalloylmannose to adsorb and immobilize the lipase. In this invention, sulfopropyl betaine anchors to the carrier surface through electrostatic, hydrogen bonding, and hydrophobic interactions, forming a hydration film to prevent pore blockage and enhance the carrier's resilience. Pentamalloylmannose permeates the pores to form a stable interpenetrating structure, giving the carrier a high specific surface area and stability. Furthermore, it stabilizes the loaded lipase through multiple interactions, preventing conformational damage and detachment of the enzyme, while simultaneously creating a stable microenvironment for the lipase, inhibiting oxidation and denaturation inactivation. The immobilized lipase prepared by this invention exhibits high catalytic activity, excellent substrate mass transfer efficiency, and good reusability, and can efficiently catalyze oleic acid esterification reactions.

The present invention relates to molecules capable of binding amyloid fibril aggregates. The present invention further describes methods for detecting the presence of amyloid fibril aggregates in a sample or subject. The present invention even further describes methods for treating pathologies caused by amyloid fibril aggregates.

Disclosures herein are directed to polypeptide probes that may be used to detect transthyretin (TTR) oligomers or fibrils in patient samples obtained from subjects with wildtype and mutant TTR alleles. Also provided are methods of using the provided probes to diagnose subjects with a TTR-associated disease or condition or for monitoring the efficacy of a therapeutic administered to treat a TTR-associated disease or condition.

Compositions for modifying or editing a polynucleotide (e.g., a gene) and methods of using the same to treat or prevent conditions associated with the extracellular deposition in various tissues of amyloid fibrils formed by the aggregation of misfolded transthyretin (TTR) proteins. Such conditions include, but are not limited to, polyneuropathy due to hereditary transthyretin amyloidosis (hATTR-PN) and hereditary cardiomyopathy due to transthyretin amyloidosis (hATTR-CM), both associated with autosomal dominant mutations of the TTR gene, and an age-related cardiomyopathy associated with wild-type TTR proteins (ATTRwt), also known as senile cardiac amyloidosis are disclosed. Compositions and methods for editing TTR polynucleotides using base editor systems are disclosed.

The invention discloses a self-healing zinc powder integrated negative electrode material and a preparation method thereof, the chemical composition expression of the material is Zn-xM-yP-zN, in the formula, x, y and z are respectively mass percentages of M, P and N, x is more than or equal to 5 and less than or equal to 15, y + z is more than or equal to 5 and less than or equal to 15, y is more than or equal to z, and the balance is Zn, M is an MBenes material, P is protein, and N is N-carboxyl anhydride; the material is obtained by mixing zinc powder subjected to acid treatment with a protein solution to prepare amyloid fiber composite zinc powder, then adding the amyloid fiber composite zinc powder into an MBenes solution, performing ultrasonic stirring, then dropwise adding an N-carboxyl anhydride solution containing a quaternary ammonium carboxylate initiator, and performing secondary ultrasonic stirring. The preparation method is simple, the process is easy to control, and the prepared material has the characteristics of self-healing, high mechanical strength, strong binding force, excellent cycling stability and the like, and can be widely applied to the fields of wearable equipment, electric automobiles and the like.

Compositions for modifying or editing a polynucleotide (e.g., a gene) and methods of using the same to treat or prevent conditions associated with the extracellular deposition in various tissues of amyloid fibrils formed by the aggregation of misfolded transthyretin (TTR) proteins. Such conditions include, but are not limited to, polyneuropathy due to hereditary transthyretin amyloidosis (hATTR-PN) and hereditary cardiomyopathy due to transthyretin amyloidosis (hATTR-CM), both associated with autosomal dominant mutations of the TTR gene, and an age-related cardiomyopathy associated with wild-type TTR proteins (ATTRwt), also known as senile cardiac amyloidosis are disclosed. Compositions and methods for editing TTR polynucleotides using base editor systems are disclosed.