30 results about "Fibrillogenesis" patented technology

Assay-guided affinity fractionation and reverse phase high pressure liquid chromatography (HPLC) methodology to isolate, test and characterize the most active water-soluble ingredients within Cat's Claw, or Uncaria tomentos. These components appear to account for the majority of the amyloid or Aβ fibrillogenesis inhibitory activity. Individual fractions and / or compounds as isolated by HPLC are tested in relevant in vitro and / or animal models, and found to consistently demonstrate inhibition of amyloid or Aβ fibrillogenesis. Related extraction methods are disclosed.

A pharmaceutical composition, or pharmaceutical agent for treating Aβ amyloidosis in a patient, having at least one selected laminin peptide or fragment thereof from the group AG73 (SEQ ID NO:1), C-16 (SEQ ID NO:2), A-13 (SEQ ID NO:3), HA3G47 (SEQ ID NO:4), HA3G58 (SEQ ID NO:5), HA3G67 (SEQ ID NO:6), HA3G74 (SEQ ID NO:7), HA3G76 (SEQ ID NO:8), HA3G79 (SEQ ID NO:9), HA3G83 (SEQ ID NO:10), A4G82 (SEQ ID NO:11), A5G15 (SEQ ID NO:12), A5G56 (SEQ ID NO:13), A5G80 (SEQ ID NO:14), A5G81 (SEQ ID NO:15), A5G82 (SEQ ID NO: 16), A5G84 (SEQ ID NO:17), A5G101 (SEQ ID NO:18), and A5G109 (SEQ ID NO:19) (Sequence Group A); and a method for enhancing Aβ amyloid fibril formation, or of forming amyloid-plaque like deposits in vitro, including incubating Aβ 1-40 or Aβ 1-42 with a selected laminin-derived polypeptide from the group A-13 (SEQ ID NO:3), HA3G47 (SEQ ID NO:4), HA3G58 (SEQ ID NO:5), HA3G83 (SEQ ID NO:10), LAM-L (SEQ ID NO:20), A4G10 SEQ ID NO:21), A4G46 (SEQ ID NO:22), A4G47 (SEQ ID NO:23), A4G84 (SEQ ID NO:24), A4G92 (SEQ ID NO:25), A4G107 (SEQ ID NO:26), A5G3 (SEQ ID NO:27), A5G10 (SEQ ID NO:28), A5G27 (SEQ ID NO:29), A5G33 (SEQ ID NO:30), A5G65 (SEQ ID NO:31), A5G77 (SEQ ID NO:32), A5G87 (SEQ ID NO:33), A5G90 (SEQ ID NO:34) and A5G111 (SEQ ID NO:35) (Sequence Group C).

The disclosure relates to a platform of using zebrafish in screening candidates for treating and / or preventing myopia and keratoconus disease. The disclosure is mainly based on that Lumican, one of several SLRPs, plays an important role in the regulation of fibrillogenesis or the genes affecting the size of eyeballs in zebrafish, in addition to playing an important role in clinical myopia. Therefore, the disclosure uses the established zebrafish model to further identify the drugs affecting the expression of lumican and collagen fibrillogenesis, and / or the regulation of eyeball size. These drugs are potential candidates for treating myopia and / or keratoconus disease.

α2-macroglobulin-related agents for treating or preventing a fibrotic disorder associated with fibrillogenesis are disclosed along with methods for using the agents, as well as methods for producing agents suited for use in the disclosed methods for treating or preventing a fibrotic disorder.

A pharmaceutical composition comprising peptide A5G81Ala-Gly-Gln-Trp-His-Arg-Val-Ser-(SEQ ID NO: 15)Val-Arg-Trp-Gly.

The present invention relates to peptides of general formula (I) capable of regulating fibrillogenesis, stereoisomers thereof and mixtures thereof, which may or may not be racemic, and the cosmetically or dermopharmaceutically acceptable salts thereof, wherein Z is alanyl, allo-isoleucyl, glycyl, isoleucyl, isoseryl, isovalyl, leucyl, norleucyl, norvalyl, prolyl, seryl, threonyl, allo-threonyl or valyl; n and m may vary between 1 and 5; AA is selected from the group consisting of natural amino acids encoded in their L- or D-form and non-encoded amino acids; x and y may vary between 0 and 2; R1 is H or alkyl, aryl, aralkyl or acyl group; and R2 is amino, hydroxyl or thiol, all of them substituted or non-substituted with aliphatic or cyclic groups. A method for obtaining cosmetic or dermopharmaceutical compositions containing them and use thereof for treating the skin, preferably those skin conditions which require regulating fibrillogenesis, such as aging and / or the softening of the appearance of scars.

A pharmaceutical composition comprising peptide A-13 Arg-Gln-Val-Phe-Gln-Val-Ala-Tyr-Ile-Ile-Ile-Lys-Ala (SEQ ID NO:3).

The present invention provides a therapeutic method for removing amyloid fibrils from a patient. The present invention also provides a transgenic animal that develops systemic AA amyloidosis within three weeks for use as a tool to investigate AA amyloidosis and to evaluate agents that may be potentially useful in preventing and treating amyloid-related disorders. Further, the present invention provides diagnostic assays for monitoring immunoglobulin light chain fibrillogenesis in real-time and for identification of the chemical nature of the protein in amyloid deposits which enables the determination of the type of amyloidosis for therapeutic and prognostic purposes.

The invention provides monomeric and oligomeric amyloid beta peptide isomers that are resistant towards fibrillogenesis and their use as screening reagents or antigens in methods and pharmaceutical preparations for the treatment of Alzheimer's disease and other conditions related to protein misfolding. The alanines at positions 21 and 30, in wild type amyloid beta peptide amino acid sequence, are according to the invention replaced by cysteins, which results in an intra molecular disulphide bond. The invention further provides transgenic animals expressing modified amyloid precursor proteins or amyloid beta peptides.

The invention relates to an osteogenic composite matrix consisting of collagen and non-collagen components of an extracellular matrix (ECM-components), to a method for producing said matrix, to a method for producing an implant or a scaffold for tissue engineering which is provided with a coating formed by said osteogenic composite matrix and is used for stimulating and accelerating a hard tissue formation such as, for example. The implant osseointegration in bones. The inventive osteogenic composite matrix comprises a collagen and at least one non-collagen ECM component or the derivatives thereof, wherein the collagen component consists of non-crosslinked collagen fibres produced by fibrillogenesis and the non-collagen ECM component or the derivatives thereof are integrated into said collagen fibres.