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Polymeric complements to [beta]-amyloid peptides

A polymer, amyloid technology, applied in the direction of peptides, peptide sources, specific peptides, etc., can solve the problems of high cost or production, lack of practical and stable methods for accurate quantification of Aβ42, low concentration, etc.

Inactive Publication Date: 2013-08-21
伯耶·塞勒格伦
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  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

However, a practical and stable method for the precise quantification of Aβ42 is still lacking
First, the protein is found in very low concentrations in the blood, requiring sensitive methods
Another difficulty in antibody-based approaches is the masking of the Aβ42 epitope by binding to plasma proteins or by Aβ oligomerization
Corresponding diagnostic methods are therefore far from immediate results, generally due to insufficient selectivity, high costs or production problems

Method used

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  • Polymeric complements to [beta]-amyloid peptides
  • Polymeric complements to [beta]-amyloid peptides
  • Polymeric complements to [beta]-amyloid peptides

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0067] Example 1: The target is Aβ42 or Aβ40 C-terminal MIP

[0068] The complement MIP of Aβ42 was prepared in the following manner: Ac-GGVVIA (SEQ ID NO: 10) (8 mg), N-3,5-bis(trifluoromethyl)-phenyl-N'-4-vinylbenzene Urea (TFU) (5mg), tetrabutylammonium (TBA) chloride (2M) dissolved in methanol (2μL), and 2-aminoethyl acrylate (AEMA) hydrochloride (235mg) dissolved in DMSO ( 600μL) and ACN (900μL). Then divinylbenzene (DVB) (930 μL) and free radical initiator ABDV (12.0 mg, 1% (w / w) total monomer) were added. After dissolution, transfer the solution to a glass test tube, cool to 0°C, and bubbling nitrogen for 10 minutes. Subsequently, the glass test tube was sealed, and polymerization was thermally initiated by placing the test tube in a water bath set at 50°C. The polymerization was carried out at this temperature for 48 hours. The test tube is then broken, and the MIP monolith is broken into smaller pieces. The template molecules were removed by the following successiv...

Embodiment 2

[0070] Example 2: The target is Aβ42 or Aβ40 C-terminal MIP

[0071] The complement MIP of Aβ42 was prepared by the following method: Ac-GGVVIA (8mg) was dissolved in methanol (2μL) of tetrabutylammonium (TBA) chloride (2M) and 2-aminoethyl acrylate (AEMA) hydrochloric acid Salt (235mg) was dissolved in DMSO (600μL) and ACN (900μL). Then add divinylbenzene (DVB) (930μL) and free radical initiator ABDV (12.0mg, 1% (w / w) total monomer), after dissolving, transfer the solution to a glass test tube and cool to 0 ℃, and nitrogen gas for 10 minutes. Subsequently, the glass test tube was sealed, and polymerization was thermally initiated by placing the test tube in a water bath set at 50°C. The polymerization was carried out at this temperature for 48 hours. The test tube is then broken, and the MIP monolith is broken into smaller pieces. The template molecules were removed by the following successive washing steps: MeOH (100 mL), MeOH / water (0.1M HCl) (90 / 10, v / v) (100 mL) and fin...

Embodiment 3

[0073] Example 3: The target is Aβ42 or Aβ40 C-terminal MIP

[0074] The complement MIPs of Aβ40 and Aβ42 were prepared in the same manner as described in Example 1 or 2 above, except that N-(2-aminoethyl)methacrylamide (AEMAM) (235mg) was used instead of 2-aminoethyl. Acrylate hydrochloride.

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Abstract

The present invention relates to the preparation and use of polymer complements to [beta]-amyloid peptides [Alpha][beta] for detecting soluble or aggregated [Alpha][beta] in fluid samples or for treating a subject having a neurodegenerative disease.

Description

Technical field [0001] This application relates to the preparation and use of the polymer complement of β-amyloid peptide (Aβ), which is used to detect soluble or polymerized Aβ in a liquid sample, or to treat patients with neurodegenerative diseases. Background technique [0002] Alzheimer's disease (AD) is the most common cause of dementia in humans in later life, and the fourth leading cause of death in developed countries. It is believed that the brain deposition of amyloid plaques plays a major role in the disease. Therefore, under the microscope, AD is characterized by significant degeneration of neurons and their synapses, as well as a large number of senile plaques and neuromyofibrillar tangles in the neocortex and hippocampus of the brain. Plaques are composed of amyloid deposits, mainly containing 39-42 residue peptides, called: β-starch (Aβ) ( figure 1 ) Aggregation. The peptide is derived from the proteolytic cleavage of the transmembrane protein amyloid precursor p...

Claims

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Application Information

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Patent Type & Authority Applications(China)
IPC IPC(8): B01J20/26C07K14/47G01N33/68
CPCC07K14/4711C07K17/14G01N33/6896G01N2800/2821B01J20/268A61K49/12A61K51/065
Inventor 伯耶·塞勒格伦卡拉·索菲亚·安图内斯-奥雷利亚诺泽维尔·羽拉萨-鲁兹埃里克·施林格
Owner 伯耶·塞勒格伦
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