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

Medicine combination containing fusion protein for suppressing angiogenesis and application

A fusion protein and angiogenesis technology, which is applied in the direction of drug combination, non-active ingredient medical preparations, pharmaceutical formulas, etc., can solve the problems of reduced protein activity, poor stability of fusion protein, and decreased therapeutic effect

Active Publication Date: 2012-03-21
CHENGDU KANGHONG BIOTECH
View PDF4 Cites 17 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

As we all know, the stability of generally recombinant fusion proteins is relatively poor, and will be affected by various environmental factors during storage, such as temperature, moderate, oxygen, ultraviolet rays, etc., which can cause various physical or chemical changes in the fusion protein, resulting in Protein aggregation, decomposition, oxidation or denaturation, etc.
These changes can reduce the activity of the protein, reduce the therapeutic effect and cause serious side effects

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
  • Medicine combination containing fusion protein for suppressing angiogenesis and application
  • Medicine combination containing fusion protein for suppressing angiogenesis and application
  • Medicine combination containing fusion protein for suppressing angiogenesis and application

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0029] Example 1 Stability study of the original formulation of 10mg / ml FP3 fusion protein in 3ml glass ampoule at 4°C

[0030] The prescription is as follows:

[0031] FP3 fusion protein 10mg / ml

[0032] Sodium succinate 10mM

[0033] Trehalose 9.0%

[0034] Tween 20 0.05%

[0035] Adjust the pH of the system to 6.0-6.5 with hydrochloric acid

[0036] After changing the protein stock solution, aseptically dispense it into 3ml glass ampoules, reserve samples at 4°C, and measure at 0, 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, and December Samples, stability determined by SEC-HPLC. The results showed that the formulation could not effectively inhibit the formation of polymers, resulting in a decrease in product purity and a decrease in affinity with VEGF, which may induce an immune response after entering the body.

[0037] Table 1.10mg / ml FP3 fusion protein stability at 4°C

[0038] time (month)

Embodiment 2

[0039] Example 2 Stability study of 10mg / ml FP3 fusion protein in 3ml glass ampoule at 4°C

[0040] FP3 fusion protein 10mg / ml

[0041]Disodium hydrogen phosphate 10mM

[0042] Sucrose 10%

[0043] Sodium chloride 0.5%

[0044] Tween 20 0.05%

[0045] pH 7.5~8.3

[0046] After changing the protein stock solution, aseptically dispense it into 3ml glass ampoules, reserve samples at 4°C, and measure at 0, 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, and December Samples, stability determined by SEC-HPLC. The results showed that the formulation could not effectively inhibit the formation of polymers, resulting in a decrease in product purity and a decrease in affinity with VEGF, which may induce an immune response after entering the body.

[0047] Table 2.10mg / ml FP3 fusion protein stability at 4°C

[0048] time (month)

Embodiment 3

[0049] Example 3 Stability study of 10mg / ml FP3 fusion protein in 3ml glass ampoule at 4°C

[0050] FP3 fusion protein 10mg / ml

[0051] Citric acid 5mM

[0052] Sucrose 8.0%

[0053] Tween 20 0.05%

[0054] pH 7.5~8.3

[0055] After changing the protein stock solution, aseptically dispense it into 3ml glass ampoules, reserve samples at 4°C, and measure at 0, 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, and December Samples, stability determined by SEC-HPLC. The results showed that the formulation could not effectively inhibit the formation of polymers, resulting in a decrease in product purity and a decrease in affinity with VEGF, which may induce an immune response after entering the body.

[0056] Table 3.10mg / ml FP3 fusion protein stability at 4°C

[0057] time (month)

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 medicine combination containing fusion protein for suppressing angiogenesis and application, and particularly relates to a medicine combination containing fusion protein of an extracellular protein domain 2 (Flt-2) of a vascular endothelial growth factor (VEGF) receptor 1, extracellular protein domains 3 and 4 (KDR-3 and 4) of a VEGF receptor 2 and human normal immunoglobulin 1(G1) Fc. The medicine combination can keep the fusion protein stable, has the most outstanding advantage of capability of effectively suppressing fusion protein polymer so as to avoid reduction of purity, and accordingly keeps bioactivity of effective components.

Description

technical field [0001] The invention relates to the field of pharmaceutical preparations, and relates to a pharmaceutical composition comprising a fusion protein of VEGF receptor fragment and immunoglobulin Fc, and its medical application. Background technique [0002] With the development of modern cell and molecular biology, the role of cytokines and cell surface related molecules in ophthalmic diseases has been widely concerned and studied. VEGF is a mitogen in vascular endothelial cells that has the biological characteristics of increasing vascular permeability. VEGF is extremely important for angiogenesis in the fetal period, and its level decreases after birth. Under physiological conditions, VEGF is expressed at a low level, which is necessary for maintaining the function of blood vessels. The latest research results suggest that it plays an extensive and important role in angiogenesis-related diseases such as age-related macular degeneration (AMD) and diabetic retin...

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): A61K39/395A61K47/34A61P27/02
Inventor 柯潇郑强
Owner CHENGDU KANGHONG BIOTECH
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