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

A method for monitoring the aggregation process of β-amyloid protein using aggregation-induced luminescence

A technique for aggregation-induced luminescence and amyloid protein, applied in the fields of biomedical research and clinical detection, to achieve the effects of improved sensitivity, low production cost, and improved detection speed

Inactive Publication Date: 2011-12-14
SHANGQIU NORMAL UNIVERSITY
View PDF3 Cites 26 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

It can qualitatively or quantitatively monitor the aggregation process of β-amyloid protein, and it will be used in the pathological diagnosis of patients with senile dementia in the latent stage. It has a good application prospect and has not yet been reported in the relevant literature

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
  • A method for monitoring the aggregation process of β-amyloid protein using aggregation-induced luminescence
  • A method for monitoring the aggregation process of β-amyloid protein using aggregation-induced luminescence
  • A method for monitoring the aggregation process of β-amyloid protein using aggregation-induced luminescence

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0028] Example 1 The aggregation process of β-amyloid protein 42 is monitored by fluorescent probe 1 coupled with maleimide, which is achieved by the following steps:

[0029] 1. Synthesis of fluorescent probe 1 coupled with maleimide, which is water-soluble. The synthetic route is shown below.

[0030] 2. Purchase Aβ42 whose glycine at position 2 is mutated into cysteine, and dissolve it in phosphate buffer solution (0.2 M, pH 7.4).

[0031] 3. Add maleimide-coupled fluorescent probe 1 in the above step 2, and use the specific covalent bond formed between the maleimide and the sulfhydryl group on cysteine ​​to specifically bind the β-amyloid protein binding to aggregation-inducing fluorescent probes.

[0032]4. Using aggregation-induced luminescence enhancement to monitor the aggregation process of β-amyloid protein: put the prepared probes into a mixture containing 50 nM Aβ42 and 400 times complement C3, complement C4, IGA, IGM, IGG, IGD, IGE, fibroblast Cell growth facto...

Embodiment 2

[0036] Example 2 The aggregation process of β-amyloid protein 42 is monitored by fluorescent probe 2 coupled with lymide, which is achieved by the following steps:

[0037] 1. Synthesis of fluorescent probe 2 coupled with maleimide, the probe is water-soluble. The synthetic route is shown below.

[0038] 2. Purchase Aβ42 whose glycine at position 2 is mutated into cysteine, and dissolve it in phosphate buffer solution (0.2 M, pH 7.4).

[0039] 3. In the above step 2, add a fluorescent probe 2 coupled with maleimide, and use the specific covalent bond formed between the maleimide and the sulfhydryl group on cysteine ​​to convert the β-amyloid specific binding to aggregation-inducing fluorescent probes.

[0040] 4. Use the aggregation-induced luminescence enhancement method to monitor the aggregation process of β-amyloid protein: put the prepared probes into 30 nM Aβ42 and 300 times complement C3, complement C4, IGA, IGM, IGG, IGD, IGE, Fibroblast growth factor, epidermal gro...

Embodiment 3

[0044] Example 3 The aggregation process of β-amyloid protein 42 is monitored by fluorescent probe 3 coupled with maleimide, which is achieved by the following steps:

[0045] 1. Synthesis of maleimide-coupled fluorescent probe 3, which is water-soluble. The synthetic route is shown below.

[0046] 2. Purchase Aβ42 whose glycine at position 2 is mutated into cysteine, and dissolve it in phosphate buffer solution (0.2 M, pH 7.4).

[0047] 3. Add the maleimide-coupled fluorescent probe 3 in the above step 2, and use the specific covalent bond formed between the maleimide and the sulfhydryl group on the cysteine ​​to specifically bind the amyloid beta protein binding to aggregation-inducing fluorescent probes.

[0048] 4. Use the aggregation-induced luminescence enhancement method to monitor the aggregation process of β-amyloid protein: put the prepared probes into the mixture containing 50 nM Aβ42 and 500 times complement C3, complement C4, IGA, IGM, IGG, IGD, IGE, fibroblast ...

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

The invention discloses a method for monitoring beta amyloid protein aggregation process by aggregation-induced emission, belonging to the technical field of biomedical research and clinical detection. With the method, the high affinity between sulfydryl on cysteine and maleimide is utilized to specially combine the beta amyloid protein on an aggregation-induced emission probe. The beta amyloid protein aggregation process is monitored on the basis of aggregation-induced emission enhancement phenomenon. The method has the advantages of high sensitivity, high selectivity, good stability, low manufacture cost and the like and is easy to control. The A beta42 and A beta40 contents can be monitored in a micromole, even a nano-mole level, the detection speed of the method is improved by 15 times if being compared with that of the detection method which utilizes probes, such as ANS (8-aniline-1-naphthalene sulfonic acid) and the like. The beta amyloid protein aggregation process can be qualitatively and quantitatively monitored, the method has a good application prospect if being applied to the pathologic diagnosis of latent patients suffering from senile dementia.

Description

technical field [0001] The invention relates to a monitoring method for the aggregation process of amyloid beta protein, in particular to a method for monitoring the aggregation process of amyloid beta protein by using an aggregation-induced luminescence method, and belongs to the technical field of biomedical research and clinical detection. Background technique [0002] Alzheimer's disease (AD) is the most common disease causing senile dementia. Currently, AD is the fourth leading killer of the elderly after cardiovascular and cerebrovascular diseases, cancer, and stroke. The pathological feature of AD is that extracellular senescent plaques and intracellular neurofibrillary tangles can be observed in the patient's brain, which is due to the abnormal aggregation of β-amyloid (amyloid β-protein, Aβ) in and out of cells. Knots can form aggregates of short peptides that are toxic to neuronal cells. The most common Aβ in plasma, cerebrospinal fluid, and short peptide aggrega...

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): G01N33/68G01N33/58
Inventor 瞿鹏宋胜梅徐茂田王永祥朱旭王静
Owner SHANGQIU NORMAL UNIVERSITY
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

Browse by: Latest US Patents, China's latest patents, Technical Efficacy Thesaurus, Application Domain, Technology Topic, Popular Technical Reports.

© 2024 PatSnap. All rights reserved.Legal|Privacy policy|Modern Slavery Act Transparency Statement|Sitemap|About US| Contact US: help@patsnap.com