Modified insulin with reduced immunogenicity

An immunogenicity and insulin technology, applied in the direction of insulin, hormone peptides, medical preparations containing active ingredients, etc., can solve the problems of not recognizing the importance of T-cell epitope protein immunogenicity

Inactive Publication Date: 2004-08-25
MERCK PATENT GMBH
View PDF11 Cites 1 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

[0016] Modified insulin molecules have also been disclosed [US, 5,700,662, US, 5,698,669; US 5,747,642; US 5,693,609], but these teachings, and other uncited examples, do not recognize that T-cell epitopes are immune to the protein The importance of the originality, nor can it be assumed that the protocol according to the present invention directly affects the properties of the protein in a specific and controllable manner.

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
  • Modified insulin with reduced immunogenicity

Examples

Experimental program
Comparison scheme
Effect test

Embodiment Construction

[0095] Various factors play an important role in determining the overall structure of a protein or polypeptide. The first is the peptide bond, the bond that links amino acids together to form a chain, which is a type of covalent bond. This bond is planar and essentially a substituted amide. "Amide" means any of a group of organic compounds containing a -CONH- group.

[0096] Planar peptide bonds linking Cα of adjacent amino acids are shown below:

[0097]

[0098] Since the O=C and C-N atoms lie in a relatively rigid plane, free rotation along these axes does not occur. Therefore, the plane shown by the dotted line in the figure is sometimes referred to as the "amide" plane or the "peptide plane", where the oxygen (O), carbon (C), nitrogen (N) and hydrogen (H) atoms of the peptide backbone are located . The Cα atoms are located at opposite corners in the amide plane. Since the O=C and C-N atoms in the plane of the peptide or amide do not substantially rotate, the polyp...

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 polypeptides to be administered especially to humans and in particular for therapeutic use. The polypeptides are modified polypeptides whereby the modification results in a reduced propensity for the polypeptide to elicit an immune response upon administration to the human subject. The invention in particular relates to the modification of human insulin to result in insulin proteins that are substantially non-immunogenic or less immunogenic than any non-modified counterpart when used in vivo.

Description

field of invention [0001] The present invention relates especially to polypeptides for administration to humans, especially for use in therapy. The polypeptide is a modified polypeptide, wherein the modification renders the polypeptide less prone to elicit an immune response when administered to a human. In particular, the invention relates to the modification of human insulin to produce insulin protein variants which are substantially non-immunogenic or less immunogenic than the unmodified corresponding protein when used in vivo. The present invention also relates to T-cell epitope peptides derived from the above-mentioned unmodified proteins, whereby insulin variants with reduced immunogenicity can be constructed. Background of the invention [0002] There are many examples where the efficacy of therapeutic proteins is limited by interfering immune responses directed against them. Several mouse monoclonal antibodies have shown promise for the treatment of a variety of hu...

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): C12N15/09A61K38/00A61K38/28A61K48/00A61P3/10A61P5/48C07K7/06C07K7/08C07K14/62C12N15/17C12P21/02
CPCC07K14/62A61K38/00A61P3/10A61P5/48
Inventor F·J·卡尔G·卡特
Owner MERCK PATENT GMBH
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