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

Refining method of ophthalmic protein medicine

A buffer solution and cation exchange technology, which is applied in the preparation method of peptides, animal/human proteins, drug combinations, etc., can solve the problems that have not yet revealed the specific conditions

Pending Publication Date: 2022-03-18
参天堂制药株式会社(韩国)
View PDF0 Cites 0 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

However, specific conditions for performing chromatography for the purification of highly pure aflibercept (or aflibercept biosimilar) substances have not been revealed

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
  • Refining method of ophthalmic protein medicine
  • Refining method of ophthalmic protein medicine
  • Refining method of ophthalmic protein medicine

Examples

Experimental program
Comparison scheme
Effect test

example 1

[0083]

[0084] (1) Cation exchange chromatography

[0085] Cation exchange chromatography was performed on aflibercept sample solutions collected by protein A affinity chromatography or from aflibercept sample solutions collected by performing protein A affinity chromatography and multimodal chromatography together to purify only the Aflibercept substance of electric point value.

[0086] Examples of charged functional groups with cation exchange resins used in the present invention can be carboxymethyl (CM), sulfoethyl (SE), sulfopropyl (SP), phosphate (P), etc., cation exchange resins Examples of carriers can be polystyrene, polystyrene / divinylbenzene, cellulose, dextran, agarose, and Toyopearl. Examples of cation exchangers used in the present invention have carboxymethyl groups (CM) in particular.

[0087] Any buffer solution that may have buffering capacity can be used as the buffer solution used in the cation exchange chromatography process of the present invention,...

example 2

[0104]

[0105] (1) Anion exchange chromatography

[0106] Anion-exchange chromatography was performed on aflibercept sample solutions collected by protein A affinity chromatography or from protein A affinity chromatography and multimodal chromatography performed together to purify only those with a specific range Aflibercept substance of electric point value.

[0107] Examples of charged functional groups with anion exchange resins used in the present invention may be amines or amino groups, more preferably primary, secondary, tertiary or quaternary amines, and most preferably tertiary or quaternary amines, the anion exchange resins Examples of carriers may be polystyrene, polystyrene / divinylbenzene, cellulose, dextran, agarose, and Toyopearl. Examples of anion exchangers used in the present invention have in particular diethylaminoethyl (DEAE) ligands and quaternary ammonium (Q) ligands.

[0108] Any buffer solution that may have buffering capacity can be used as the buf...

example 3

[0125]

[0126] Aflibercept sample solutions collected by protein A affinity chromatography or aflibercept sample solutions from protein A affinity chromatography and multimodal chromatography performed together were subjected to combined application of cation exchange chromatography and anion exchange chromatography to purify Only aflibercept substances with isoelectric point values ​​within a specific range.

[0127] That is, according to the method of Example 1 and Example 2, the chromatography with CM-Sepharose FF resin as the cation exchange resin is first performed, and then the chromatography with the Q-Sepharose FF resin as the anion exchange resin is performed, or the chromatography with the Q-Sepharose FF resin is first performed Chromatography as anion-exchange resin followed by chromatography with CM-Sepharose FF resin as cation-exchange resin allows for easier purification of chromatographic substances having only a specific range (pH 6.0-8.3) than when performin...

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 present invention relates to a method for refining ophthalmic protein drugs having isoelectric points in a specific range by applying cation exchange chromatography or anion exchange chromatography. According to the present invention, a high-purity ophthalmic protein drug can be produced more economically by applying three or four chromatography processes.

Description

technical field [0001] The present invention relates to a method for refining aflibercept used as an active ingredient of ophthalmic protein medicine. According to the present invention, aflibercept having an isoelectric point value within a specific range can be purified by performing cation exchange chromatography or anion exchange chromatography, thereby improving the quality and yield of an ophthalmic protein drug. Background technique [0002] Angiogenesis is thought to be involved in the pathogenesis of various diseases such as solid tumors, proliferative retinopathy, age-related macular degeneration (AMD) and rheumatoid arthritis. Vascular endothelial growth factor (VEGF), one of the factors required for angiogenesis, is expressed in human cancers and also plays a key role in tumor neovascularization. It is also known that high concentrations of VEGF in the eye fluid of patients with diabetes and other ischemic retinopathy are highly correlated with angiogenic activi...

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): C07K16/22C07K16/06C07K1/18A61K9/00A61K47/14A61K47/26A61P27/02
CPCA61K47/26A61P27/02C07K2319/30C07K14/71A61K9/0048A61K9/0019A61K47/12C07K16/22C07K16/065C07K1/18A61K47/14
Inventor 河秉缉朴镕涉徐美兰李在镐金东奎郑在寅
Owner 参天堂制药株式会社(韩国)
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