Check patentability & draft patents in minutes with Patsnap Eureka AI!

Tetrapeptide and application thereof

An amino acid and sequence technology, applied in the direction of peptides, specific peptides, immunoglobulins, etc., can solve problems such as ligand shedding pollution, antibody separation and purification technology needs to be improved, and Protein A/G is easy to inactivate, and achieves the effect of simple preparation

Active Publication Date: 2019-02-19
NANYANG NORMAL UNIV
View PDF3 Cites 0 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

At present, protein A / G affinity purification medium is used for the separation and purification of antibodies in industry, and there are a series of problems such as expensive medium, easy inactivation of protein A / G, difficult cleaning, ligand shedding and pollution, etc.
Antibody separation and purification technology needs to be improved urgently

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 and application thereof
  • Tetrapeptide and application thereof

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 3

[0026] Example 3 Antibody Adsorption Peptide Separation and Purification of Antibody

[0027] 1) Prepare 20mmol / L Hepes buffer solution, pH7.4, NaCl content 0.15M. Set the flow rate to 1mL / min.

[0028] 2) Use the liquid prepared in 1) as the mobile phase, and run the AKTA protein purification system.

[0029] 3) Take 2 mL of the affinity medium in Example 2 to fill the separation column.

[0030] 4) Load 2 mL of antibody IgG fermentation broth.

[0031] 5) Prepare 0.1M HCl-Gly buffer at pH 2 as the eluent.

[0032] 6) Load 6 mL of the eluate respectively, and collect the eluate.

[0033] 7) Measure the antibody content and purity in the antibody fermentation broth and the eluate of the novel separation short peptide medium, and calculate the extraction rate.

[0034] Table 1 Adsorption characteristics of the new medium for separating short peptides

[0035]

[0036] It can be seen from Table 1 that the polypeptides of the present invention can specifically bind to an...

Embodiment 4

[0037] Embodiment 4 adsorption medium preparation

[0038] 1) Dissolve 10 mg of the polypeptide prepared in Example 1 in 5 mL of Hepes buffer, pH 7.4.

[0039] 2) Take 2 mL of Sepharose gel activated by sulfhydryl group of GE Company.

[0040] 3) The above two were mixed and reacted for 8 hours.

[0041] 4) After the reaction is completed, the gel particles are washed with Hepes buffer to obtain an affinity medium.

Embodiment 5

[0042] Example 5 Antibody Adsorption Peptide Specific Adsorption Antibody

[0043] 1) Prepare 20mmol / L Hepes buffer solution, pH7.4, NaCl content 0.15M. Set the flow rate to 1mL / min.

[0044] 2) Use the liquid prepared in 1) as the mobile phase, and run the AKTA protein purification system.

[0045] 3) Take 2mL of the affinity medium and 2mL of the Protein A medium in Example 4 to fill the separation column respectively.

[0046] 4) Load 2 mL of serum respectively.

[0047] 5) Prepare 0.1M HCl-Gly buffer at pH 2 as the eluent.

[0048] 6) Load 6 mL of the eluent, respectively, and collect the effluent and eluate.

[0049] 7) Measure the antibody IgG content and purity in the serum, effluent and eluate respectively, and calculate the extraction rate.

[0050] Table 2 Adsorption characteristics of the new medium for separating short peptides

[0051]

[0052] It can be known from Table 2 that the polypeptides of the present invention can specifically bind to antibodies....

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. The amino acid sequence of the tetrapeptide is Gly-Trp-Trp-Asp. The tetrapeptide can absorb antibodies, specifically combine the anti-bodies and be used for purifying the antibodies.

Description

technical field [0001] The invention belongs to the field of biotechnology, and in particular relates to a tetrapeptide and its application. Background technique [0002] Functional peptides are a class of compounds with a molecular weight between amino acids and proteins, which have certain biological activities and can be used as drugs for treating diseases, biocatalytic levels of reactions, and ligands for specific binding. It has a wide range of applications in the fields of biology, medicine and chemical industry, and has great social and economic benefits. [0003] Affinity separation is a separation and purification method established by utilizing the characteristics of specific recognition and reversible binding of certain affinity ligands to biomacromolecules. Usually only one step of processing is needed to obtain a certain protein with higher purity. Affinity ligands are the core of affinity separation, so the development of corresponding functional peptides is ...

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): C07K5/103C07K16/00
CPCC07K5/1008C07K16/00
Inventor 韦宇平张鑫张浩李娜滕伯远
Owner NANYANG NORMAL UNIV
Features
  • R&D
  • Intellectual Property
  • Life Sciences
  • Materials
  • Tech Scout
Why Patsnap Eureka
  • Unparalleled Data Quality
  • Higher Quality Content
  • 60% Fewer Hallucinations
Social media
Patsnap Eureka Blog
Learn More