Unlock instant, AI-driven research and patent intelligence for your innovation.
A small molecule antibody affinity peptide and its application
What is Al technical title?
Al technical title is built by PatSnap Al team. It summarizes the technical point description of the patent document.
A small molecule antibody and affinity peptide technology, applied in the field of molecular biology, can solve the problems of reduced separation effect, high production cost, unstable protein A, etc.
Inactive Publication Date: 2018-03-23
INST OF PROCESS ENG CHINESE ACAD OF SCI
View PDF2 Cites 0 Cited by
Summary
Abstract
Description
Claims
Application Information
AI Technical Summary
This helps you quickly interpret patents by identifying the three key elements:
Problems solved by technology
Method used
Benefits of technology
Problems solved by technology
[0004] 1) Expensive: Because the protein A ligand needs to be produced and purified by genetic engineering, the production cost is high, and its price reaches $10,000 / liter of affinity medium;
[0006] 3) Since the ligand is also a protein, it is easily hydrolyzed by the protease present in the raw material solution, thereby reducing the separation effect;
[0008] 5) The ligand is easy to fall off, and the fallen protein A will cause human immune response and has been clinically proven to be toxic to the human body;
[0009] 6) The elution pH is low (pH2-3), which can easily cause some antibodies to be inactivated or aggregated. It is often necessary to collect the product while neutralizing it, which increases the complexity of the operation
[0012] 2) Poor affinity: The ligand affinity of current small molecule compounds is usually lower than that of Protein A / G
[0013] 3) Poor selectivity: the current small molecule compound ligands will also bind to the main separation impurity HAS (human serum albumin) while binding to IgG
[0014] Therefore, the current separation and purification of IgG lacks an efficient, safe and economical affinity ligand
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
Click on the blue label to locate the original text in one second.
Reading with bidirectional positioning of images and text.
Smart Image
Examples
Experimental program
Comparison scheme
Effect test
Embodiment 2I
[0040] Example 2 Determination of IgG Affinity Characteristics
[0041] 1) Prepare 10mmol / L Hepes buffer, pH 7.4, NaCl content 150mmol / L.
[0042] 2) Using the liquid prepared in 1) as the mobile phase, run the Biacore T200 analyzer.
[0043] 3) Insert the detection chip CM5, and set the flow rate to 30 μL / min.
[0044] 4) Inject 100 μL of EDC and NHS in turn to activate the chip.
[0046] 6) Inject 100 μL of the IgG solution in 5), and fix the IgG on the chip surface.
[0047] 7) Small molecule antibody affinity peptide 1 (amino acid sequence shown in SEQ ID No. 11), small molecule antibody affinity peptide 2 (amino acid sequence shown in SEQ ID No. 34) and natural ligand (ProG and ProA), dissolved in 1) to prepare liquid, the content is 100μg / mL.
[0048] 8) Inject different concentrations of peptides and natural ligands in sequence (concentrations from high to low are 500 μm, 250 μm, 125 μm, 62.5 μ...
Embodiment 3
[0053] Example 3 Comparison of the adsorption properties of small molecule antibody affinity peptides with IgG and HAS
[0054] 1) Prepare 10mmol / L Hepes buffer, pH 7.4, NaCl content 150mmol / L.
[0055] 2) Using the liquid prepared in 1) as the mobile phase, run the Biacore T200 analyzer.
[0056] 3) Insert the detection chip CM5, and set the flow rate to 30 μL / min.
[0057] 4) Inject 100 μL of EDC and NHS in turn to activate the chip.
[0058] 5) Dissolve IgG in sodium acetate buffer, pH 4.5, IgG100μg / mL. Similarly, HSA was dissolved in sodium acetate buffer, pH 4.5, and HSA was 100 μg / mL.
[0059] 6) Inject 100 μL of the IgG solution in 5), and fix the IgG on the chip surface.
[0060] 7) Inject 100 μL of the HSA solution in 5) to fix HSA on the surface of another chip.
[0061] 8) Dissolve the small molecule antibody affinity peptide 3 (amino acid sequence shown in SEQ ID No. 1) and the small molecule antibody affinity peptide 4 amino acid sequence shown in SEQ ID No. ...
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
technical field [0001] The present invention relates to the field of molecular biology, in particular, the present invention relates to a small molecule antibody affinity peptide with high antibody selectivity and its application. Background technique [0002] Immunoglobulin IgG, that is, antibody is a special protein molecule, which is used as a reagent for in vitro diagnosis, a drug for the treatment of diseases, a ligand for immunoaffinity chromatography, etc. Applications. [0003] At present, the natural affinity ligand Protein A / G of the antibody is mostly used for the separation and purification of IgG. Due to the ability of Protein A / G to specifically recognize the Fc fragment of the antibody, the antibody is purified using Protein A / G affinity chromatography. The purity of the product is high. However, since Protein A / G is also an active biological substance, there are also some problems in the separation of Protein A / G: [0004] 1) Expensive: Because the protein...
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
Application Date:The date an application was filed.
Publication Date:The date a patent or application was officially published.
First Publication Date:The earliest publication date of a patent with the same application number.
Issue Date:Publication date of the patent grant document.
PCT Entry Date:The Entry date of PCT National Phase.
Estimated Expiry Date:The statutory expiry date of a patent right according to the Patent Law, and it is the longest term of protection that the patent right can achieve without the termination of the patent right due to other reasons(Term extension factor has been taken into account ).
Invalid Date:Actual expiry date is based on effective date or publication date of legal transaction data of invalid patent.
Login to View More 
Login to View More