Application of mutant single-chain human coagulation factor VIII in preparation of fusion protein

A technology of human coagulation factor and fusion protein, which is applied in the fusion protein of mutant human coagulation factor VIII and its preparation, in the field of treatment of various coagulation-related diseases, and can solve the problem of the number and structure of FVIII derivatives and the instability of thrombin activation. And other issues

Active Publication Date: 2021-07-13
AMPSOURCE BIOPHARMA (SHANGHAI) INC +1
View PDF15 Cites 2 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

[0009] In summary, although many studies have provided effective recombinant FVIII protein preparation solutions, compared with full-length FVIII, the heterologous number, structure and instability of thrombin activation of FVIII derivatives are still a serious problem.
Furthermore, since many B-domain-deleted FVIIIs are expressed as fusion proteins, new immunogenicity may emerge after administration of non-native amino acid sequences

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
  • Application of mutant single-chain human coagulation factor VIII in preparation of fusion protein
  • Application of mutant single-chain human coagulation factor VIII in preparation of fusion protein
  • Application of mutant single-chain human coagulation factor VIII in preparation of fusion protein

Examples

Experimental program
Comparison scheme
Effect test

Embodiment Construction

[0062] hCG-β carboxy-terminal peptide (CTP)

[0063] CTP is a short peptide derived from the carboxy-terminus of the β-subunit of human chorionic gonadotropin (hCG). The four reproductive-related polypeptide hormones follicle-stimulating hormone (FSH), luteinizing hormone (LH), thyrotropin (TSH) and chorionic gonadotropin (hCG) contain the same α-subunit and each specific β -subunit. Compared with the other three hormones, the half-life of hCG in vivo is significantly prolonged, which is mainly derived from the unique carboxy-terminal peptide (CTP) on its β-subunit (Fares FA et al., Proc NatlAcad Sci USA, 1992,89 (10): 4304 -4308). Native CTP contains 37 amino acid residues with 4 O-glycosylation sites terminated by sialic acid residues. Negatively charged, highly sialylated CTP can resist its clearance by the kidneys, thereby prolonging the half-life in vivo (Fares FA et al., Proc Natl Acad Sci USA, 1992, 89(10): 4304-4308). However, the present invention creatively links...

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 an application of a mutant single-chain human blood coagulation factor VIII in preparation of a fusion protein of the human blood coagulation factor VIII; the fusion protein sequentially comprises a B-structural domain partially deleted mutant single-chain human coagulation factor VIII, a flexible peptide joint, at least one human chorionic gonadotropin beta subunit carboxyl terminal peptide rigid unit and a half-life prolonging part from an N terminal to a C terminal, and is used for preventing or treating hemorrhagic diseases.

Description

technical field [0001] The present invention relates to the field of fusion proteins, more specifically, to a fusion protein of mutant human blood coagulation factor VIII (FVIII) and its preparation method and application, especially the application for treating various blood coagulation-related diseases. Background technique [0002] Coagulation factor VIII (FVIII), also known as antihemophilic factor, plays a very important role in the endogenous coagulation system. Numerous studies in the molecular genetics of FVIII have shown that a lack of FVIII in the sex chromosome X-linked gene causes hemophilia A. According to statistics, the prevalence of hemophilia A in the male population is 1 / 5000, accounting for more than 80% of the total number of hemophilias. The current commonly used treatment for hemophilia A is replacement therapy, which is to supplement the FVIII that is lacking in hemophilia patients. [0003] Mature FVIII consists of a light chain with an approximate ...

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): C07K19/00A61K38/37A61P7/04
CPCC07K14/755A61P7/04A61K38/00C07K2319/30C07K2319/31A61K38/37A61P7/00C07K14/59C07K2319/91
Inventor 高永娟贾世香郑云程金莹莹王著董炤陈思孙乃超李强
Owner AMPSOURCE BIOPHARMA (SHANGHAI) INC
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

Browse by: Latest US Patents, China's latest patents, Technical Efficacy Thesaurus, Application Domain, Technology Topic.

© 2024 PatSnap. All rights reserved.Legal|Privacy policy|Modern Slavery Act Transparency Statement|Sitemap