Antibodies that specifically bind to A beta oligomers and use thereof

A technology of oligomers and antibodies, applied in the direction of antibodies, specific peptides, drug combinations, etc., can solve the problems of difficult to measure Aβ oligomers alone, side effects, etc.

Active Publication Date: 2012-07-11
IMMUNAS PHARMA
View PDF7 Cites 6 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

In addition, antibody binding to Aβ monomers can cause side effects due to the presence of Aβ monomers in the brain of healthy individuals
[0007] In addition, the amount of Aβ oligomers can be used as an indicator of Alzheimer's disease; however, it is difficult to measure Aβ oligomers alone using conventional anti-Aβ antibodies

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
  • Antibodies that specifically bind to A beta oligomers and use thereof
  • Antibodies that specifically bind to A beta oligomers and use thereof
  • Antibodies that specifically bind to A beta oligomers and use thereof

Examples

Experimental program
Comparison scheme
Effect test

Embodiment

[4596] Hereinafter, the present invention is specifically described with reference to examples, but should not be construed as being limited thereto.

[4597] method :

[4598] Antigen preparation

[4599] The fluorescent dye 6-carboxytetramethylrhodamine (6-TAMRA) (SIGMA) was chemically linked to the N-terminus of the synthetic Aβ1-40 peptide (Peptide Institute, Inc.) to generate modified Aβ. An oligomer-rich sample (Aβ1-40 oligomer) was prepared by copolymerizing the modified Aβ and the synthetic Aβ1-40 peptide. Conditions are preferably adjusted so that the fluorescence intensity measured by the ThT assay described below (Yamamoto N, et al: J Biol Chem, 282: 2646-2655, 2007) is a quarter or less of that in the absence of modified Aβ . More specifically, it is preferable to mix 100 µM each of the modified Aβ and the synthetic Aβ 1-40 peptide, and polymerize for 20 hours.

[4600] Preparation of antibody-producing hybridomas

[4601] BALB / c mice were immunized by i...

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 inventors successfully produced monoclonal antibodies that are specific to only soluble A beta oligomers, but do not recognize soluble A beta monomers, which are physiological molecules. It was demonstrated that the antibodies are useful as diagnostic/therapeutic monoclonal antibodies for Alzheimer's disease.

Description

field of invention [0001] priority [0002] This application claims the benefit of US Provisional Application No. 61 / 231,797, filed August 6, 2009, and US Provisional Application No. 61 / 282,533, filed February 26, 2010, which are hereby incorporated by reference in their entirety. technical field [0003] The present invention relates to antibodies specifically binding to Aβ oligomers and uses thereof. Background of the invention [0004] The number of Alzheimer's disease (AD) patients worldwide exceeded about 26 million in 2006, and it is predicted to continue rising in an aging society (Non-Patent Literature (NPL) 1). However, there are no curative therapeutics that can retard or reverse the progression of Alzheimer's disease, although therapeutics that can retard disease progression are commercially available. [0005] Multiple lines of evidence have shown that memory impairment results from synaptic dysfunction triggered by soluble amyloid beta (Aβ) oligomers (see N...

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): C07K16/18A61K39/395A61P25/28C07K16/46C12N15/09C12Q1/02G01N33/53
CPCG01N33/6896G01N2800/2821C07K16/18C07K2317/33A61P25/00A61P25/28
Inventor 横关达己冈本康秀梅田真高松尚文伊藤俊行今井雪穗藤井忍
Owner IMMUNAS PHARMA
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