Tetrapeptide with function of resisting Abeta protein aggregation and application of tetrapeptide as well as gene for encoding tetrapeptide

A protein aggregation and residue technology, applied in the field of peptides, can solve problems such as lack of specificity, and achieve the effects of improving memory, delaying the disease process, and major social and economic benefits.

Inactive Publication Date: 2018-10-19
SOUTH CHINA UNIV OF TECH
View PDF6 Cites 4 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

However, in the treatment of AD, there is always a lack of effective drugs that are

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
  • Tetrapeptide with function of resisting Abeta protein aggregation and application of tetrapeptide as well as gene for encoding tetrapeptide
  • Tetrapeptide with function of resisting Abeta protein aggregation and application of tetrapeptide as well as gene for encoding tetrapeptide
  • Tetrapeptide with function of resisting Abeta protein aggregation and application of tetrapeptide as well as gene for encoding tetrapeptide

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0040] Synthesis of Peptide WW-4 by Solid Phase Synthesis of Peptide

[0041] 1. Resin selection

[0042] (1) Using the standard Fomc protocol, initially select 0.0125mmol 2-chlorotrityl chlorideresin resin (Tianjin Nankai Synthetic Technology Co., Ltd.), and add 0.3mol For the first Fmoc protection of amino acids, DCC and 5% (mass fraction) DMAP were added to the reactor to shake the reaction, and the resin was washed with methylpyrrolidone (NMP) to remove excess protected amino acids.

[0043] (2) Using the standard Fomc scheme, initially select 0.0125mmol Wang resin, according to the sequence characteristics from the C-terminal to the N-terminal of the amino acid sequence Trp-Asp-Gln-Trp, add 0.3mol of the first Fmoc protected amino acid, DCC and 5% (mass fraction) DMAP is added to the reactor to shake and react, and the resin is washed with NMP to remove excess protected amino acids.

[0044] The coupling ratios of the two resins are: 95.07% for 2-chlororityl chloride re...

Embodiment 2

[0050] Anti-Aβ42 Protein Aggregation Activity Experiment of Synthetic Polypeptide WW-4 in Vitro

[0051] 1. Experimental method

[0052] Preparation of culture medium: High glucose medium (DMEM), fetal bovine serum (FBS), L-glutamine were prepared according to the mass ratio of 8.75:1:0.25 respectively; 1wt% double antibodies (penicillin and streptomycin) were added at the same time , 0.1 wt% Hygromycin B and 0.05 wt% Blasticidin S antibiotics.

[0053] Preparation of 0.05mM and 0.5mM polypeptide (WW-4) solutions: Weigh 11.4mg of polypeptide WW-4, dissolve it with 10mL of medium, pass through a 0.22μm filter head, the concentration of the mother solution is 1mM, and then use the medium to dissolve The mother liquor was diluted to the concentration required for the experiment.

[0054] Preparation of 1 mg / mL tetracycline solution: Weigh 10 mg of tetracycline, prepare with 10 mL of PBS buffer, pass through a 0.22 μm filter head, and store at -20°C in the dark for future use. ...

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 provides a tetrapeptide with a function of resisting Abeta42 protein aggregation and application of the tetrapeptide as well as a gene for encoding the tetrapeptide. The synthetic peptide has the efficacy of obviously resisting the Abeta42 protein aggregation, and further has the effects of improving memory and delaying disease progress of Alzheimer's disease; the synthetic peptide can be widely applied to preparation of a medicine or food for resisting the Abeta42 protein aggregation, or is applied to preparation of a medicine or food for preventing or treating the Alzheimer's disease, and can further effectively prevent and treat neurodegenerative diseases including AD disease so as to improve medical conditions of the neurodegenerative diseases; the tetrapeptide has greatsocial and economic benefits.

Description

technical field [0001] The invention relates to the technical field of polypeptides, in particular to a synthetic polypeptide, its application and a gene encoding the tetrapeptide. Background technique [0002] Alzheimer's disease (AD), also known as senile dementia, is a progressive central nervous system degenerative disease with insidious onset. The clinical manifestation of AD is that the patient's intelligence declines in a conscious state, including memory, attention, calculation power, judgment, abstract thinking ability, language function, etc., as well as emotional and behavioral disorders. In the late stage of the disease, AD patients suffer from severe memory loss, inability to take care of themselves in daily life, incontinence of urine and feces, and symptoms of mutism and limb stiffness. Physical examination shows positive vertebral tract signs, primitive reflexes such as strong grasping, groping and sucking, and eventually coma. Infection and other causes of ...

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
IPC IPC(8): C07K5/117C12N15/11A61K38/07A61P25/28A23L33/18
CPCA23L33/18A23V2002/00A61K38/00A61P25/28C07K5/1024A23V2200/322A23V2250/55
Inventor 任娇艳杨柳
Owner SOUTH CHINA UNIV OF TECH
Who we serve
  • R&D Engineer
  • R&D Manager
  • IP Professional
Why Eureka
  • Industry Leading Data Capabilities
  • Powerful AI technology
  • Patent DNA Extraction
Social media
Try Eureka
PatSnap group products