Peptide having osteoclast differentiation and activation inhibition, and use of same

An activity-inhibiting, osteoclast technology, used in medical preparations containing active ingredients, peptides, bone diseases, etc.

Active Publication Date: 2017-09-01
CAREGEN
View PDF6 Cites 2 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

However, these drugs do not have the effect of promoting new bone formation. Recently, necrosis of the jaw bone (osteonecrosis), severe atrial fibrillation, weakness of bones or joints, or musculoskeletal dysfunction have occurred in patients taking bisphosphonates. Cases of pain are increasing every year

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
  • Peptide having osteoclast differentiation and activation inhibition, and use of same
  • Peptide having osteoclast differentiation and activation inhibition, and use of same
  • Peptide having osteoclast differentiation and activation inhibition, and use of same

Examples

Experimental program
Comparison scheme
Effect test

Synthetic example 1

[0046] Synthesis Example 1: Peptide Synthesis

[0047] 700 mg of Chloro trityl chloride resin (Chloro trityl chloride resin; CTL resin, Novabiochem Cat No. 01-64-0021) was put into the reaction vessel, and 10 ml of dichloromethane (MC) was added to stir for 3 minutes . The solution was removed and 10 ml of dimethylformamide (DMF) was added to stir for 3 minutes, and the solvent was removed again. The dichloromethane (DCM) solution of 10ml is put into reactor, and put into the Fmoc-Arg (Pbf)-OH (Swiss Bachem (Bachem, Swiss)) of 200mmol and the diisopropylethylamine of 400mmol ( DIEA), stirred and dissolved uniformly, stirred for 1 hour and reacted. Wash after the reaction, dissolve methanol and diisopropylethylamine (2:1) in dichloromethane, react for 10 minutes, and wash with excess dichloromethane / dimethylformamide (1:1). The solution was removed and 10 ml of dimethylformamide was added to stir for 3 minutes, and the solvent was removed again. 10 ml of a deprotection solu...

Embodiment 1

[0053] Example 1: Tartrate-resistant acid phosphatase staining

[0054] The degree of tartrate-resistant acid phosphatase protein expressed when osteoclasts were differentiated was confirmed by staining, and the tendency to decrease when the peptide was treated was observed.

[0055] Take 1×10 4 After seeding Raw264.7 macrophages in a 48-well plate, the cells / well were simultaneously treated with peptides (independent peptides or 50 ng / ml NF-KB receptor activator ligand simultaneously) by concentration, and Differentiation was induced by culturing for 5 days. Staining for tartrate-resistant acid phosphatase was performed using the acid phosphatase kit from Sigma aldrich. After adding the fixation buffer, the reaction was performed for 30 seconds, followed by washing with distilled water. 200 µl of staining solution was placed in each well, reacted at 37° C. for 30 minutes, and washed with distilled water. Observation was carried out with a microscope after drying for one d...

Embodiment 2

[0057] Example 2: Reverse transcription-polymerase chain reaction related to tartrate-resistant acid phosphatase and cathepsin K (cathepsin K)

[0058] The mRNA levels of tartrate-resistant acid phosphatase and cathepsin K (mRNA level) expressed when osteoclasts were differentiated were confirmed by reverse transcription-polymerase chain reaction, and observed when peptides were treated tendency to decrease.

[0059] Take 1×10 4 Cell Density of Cells / well RAW 264.7 macrophages were seeded in 48-well plates. At the same time, 50 ng / ml of nuclear factor KB receptor activator ligand and peptide were treated at concentrations (10 μg / ml, 50 μg / ml), and cultured in a 37° C. incubator for 5 days. After recovering the cultured cells, RNA was prepared by treating RNA extraction solution (Easy Blue, Intron) and then synthesized using antisense premix (RTpremix) (Intron) Complementary deoxyribonucleic acid (cDNA). Polymerase chain reaction was performed by using primers for the respe...

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

A peptide which is formed from an amino acid sequence selected from the group comprising amino acid sequences of SEQ ID NO: 1 and SEQ ID NO: 3, according to the present invention, has osteoclast differentiation and activation inhibition and is highly effective for preventing or treating bone diseases related to the destruction of the bone. A peptide, according to the present invention, reduces expression of cathepsin K and TRAP related to osteoclast differentiation, inhibits nuclear translocation of NF-kB, and ultimately inhibits osteoclast differentiation. Provided is a composition, for preventing or treating bone diseases, comprising the peptide.

Description

technical field [0001] This patent application claims priority to Korean Patent Application No. 10-2014-0098362 filed with the Korean Patent Office on July 31, 2014, and the disclosures of the above patent application are incorporated herein by reference. [0002] The present invention relates to a peptide capable of inhibiting osteoclast differentiation and activity and its use. Background technique [0003] Bones serve to support the body's soft tissues and body weight, and surround internal organs to protect them from external shocks. And, it is one of the important parts of the human body that not only supports muscles or organs structurally, but also stores calcium or other essential inorganic substances in the body, that is, stores substances such as phosphorus or magnesium. As a result, the bones of an adult adult at the end of growth undergo a very dynamic, continuous regeneration process of removing old bone and replacing it with new bone until death, in a balanced...

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): C07K7/06A61K38/08A61P19/00
CPCA61K38/08C07K7/06A61K38/00A61P19/00
Inventor 郑镕池金银美李应智A·R·韩韩美丽
Owner CAREGEN
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