Looking for breakthrough ideas for innovation challenges? Try Patsnap Eureka!

Compositions and methods for the treatment of "plaques and tangles" in humans and animals

一种组合物、斑块的技术,应用在药物组合、医药配方、植物原材料等方向

Pending Publication Date: 2021-08-24
COGNITIVE CLARITY INC
View PDF4 Cites 0 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

There are currently no drugs approved to reduce and remove beta-amyloid "plaques" and tau-containing "tangles" in the brain

Method used

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
View more

Image

Smart Image Click on the blue labels to locate them in the text.
Viewing Examples
Smart Image
  • Compositions and methods for the treatment of "plaques and tangles" in humans and animals
  • Compositions and methods for the treatment of "plaques and tangles" in humans and animals
  • Compositions and methods for the treatment of "plaques and tangles" in humans and animals

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0175] Example 1: Destruction / inhibition of Alzheimer's disease Aβ fibrils or aggregates

[0176] The compositions described herein were found to be potent disruptors / inhibitors of A[beta] protein fibrils or aggregates. This example investigates the efficacy of the composition in causing the breakdown / disruption / depolymerization of pre-formed amyloid fibrils (ie, consisting of Aβ1-42) of Alzheimer's disease.

[0177] Part A: Thioflavin T fluorescence method

[0178] In this study, the effect of the composition was determined using Thioflavin T fluorescence. Thioflavin T specifically binds to fibril amyloid, and this binding produces a fluorescence increase at 485 nm that is proportional to the number of amyloid fibrils formed. The higher the fluorescence, the more the number of amyloid fibrils formed (Nakai et al., Lab.Invest.65:104-110, 1991; Levine III, Protein Sci.2:404-410, 1993; Amyloid: Int. J. Exp. Clin. Invest. 2:1-6, 1995).

[0179] In this study, 40 μl of a 1 mg / ...

Embodiment 2

[0209] Example 2: Inhibition / Disruption of In Vitro Conversion of Aβ to β-Sheets Containing Fibrillar Structures Part A: Thioflavin T Fluorometric Assay

[0210] To test whether the compositions described herein can inhibit β-sheet formation of Aβ, the same Thioflavin T assay as described in Example 1 was utilized, but using Aβ1-40 as substrate instead. Similar to Aβ1-42, Aβ1-40 forms Thioflavin T-positive aggregates but requires >24 hours of incubation at 37°C with shaking to fully fibrillate. Since A[beta]1-40 is in a non-fibrillar state at the start of the assay, this protein can be aggregated in the presence of the composition to measure aggregation inhibition. Lyophilized human Aβ1-40 (rPeptide) was dissolved in dH20 to 1 mg / mL (220 μΜ). In separate tubes, different concentrations of test composition stock solutions were prepared in PBS such that a final reaction containing equal volumes of test composition stock solutions and Aβ solution would yield a final Aβ concentra...

Embodiment 3

[0218] Example 3: In vitro screening of tau aggregation inhibitors using recombinant Tau repeat domains

[0219] In previous studies on in vitro screens for the identification of tau aggregation inhibitors, the present inventors found that, under the same experimental conditions, paired helical filaments were formed from commercially available full-length tau protein (Tau441; from rPeptide). Filament (PHF) (>11 days; data not shown) is much slower than formation of paired helical filaments (>24 hours) by tau repeat domains (TauRD; Q244-E372 containing Tau441) (S. Barghorn et al. , Methods Mol Biol, 299:35-51, 2005).

[0220] Due to its apparently short turnaround time and common aggregation properties, TauRD was used to screen tau aggregation inhibitors in vitro. Since TauRD protein is not commercially available, TauRD was prepared according to the following procedure, which is also described in US 2016 / 0250273 (where the disclosure for this procedure is incorporated by refer...

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
Login to View More

PUM

No PUM Login to View More

Abstract

Composition and methods for treating brain "plaques" and / or "tangles" in a subject wherein the method comprises administration of a therapeutically effective amount of a composition comprising a black currant extract, Uncaria tomentosa extract, and an oolong tea extract.

Description

[0001] related application [0002] This application claims the benefit of priority to U.S. Provisional Application 62 / 778,875, filed December 12, 2018, which is incorporated herein by reference in its entirety. technical field [0003] The present invention relates to mixture compositions of plant extracts of black currant, Uncaria tomentosa and oolong tea, and the use of such compositions in the treatment of amyloidosis and tauopathies in humans and animals, such as elderly dogs and cats How 'plaques' and 'tangles' build up in the aging brain. Furthermore, the present invention relates to the development of a nutritional blend composition consisting of a combination of black currant extract, Uncaria tomentosa plant extract and oolong tea extract for the prevention and treatment of traumatic brain injury (TBI), concussion (as in most observed in athletes and military / soldiers), single and repeated blows to the head, and chronic traumatic encephalopathy (CTE). Finally, the p...

Claims

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
Login to View More

Application Information

Patent Timeline
no application Login to View More
Patent Type & Authority Applications(China)
IPC IPC(8): A61K36/185A61K36/74A61K36/82A61P25/00A61P25/28A61P3/00
CPCA61P25/28A61K36/82A61K36/74A61K36/185A61K9/4841A61K2300/00A61K9/48A61K9/0095
Inventor A·斯诺
Owner COGNITIVE CLARITY INC
Who we serve
  • R&D Engineer
  • R&D Manager
  • IP Professional
Why Patsnap Eureka
  • Industry Leading Data Capabilities
  • Powerful AI technology
  • Patent DNA Extraction
Social media
Patsnap Eureka Blog
Learn More
PatSnap group products