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

Affinity small molecules for the EPO receptor

Inactive Publication Date: 2004-06-17
F HOFFMANN LA ROCHE & CO AG
View PDF1 Cites 3 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

In many situations, the level of treatment is compromised by the adverse effect on the red blood cell count, so that the desired therapy cannot be administered.
EPO is a large glycosylated protein that is expensive and difficult to manufacture, purify and formulate.
It is also degraded by proteases when in the blood, so that a substantial portion of the administered EPO is lost.
However, the peptide is small and will be rapidly degraded in the blood.
Also, it suffers from the inconvenience of requiring injection.
When a patient suffers from acute renal failure or when chronic renal failure develops, the inadequate renal production of erythropoietin results in hypoplastic anemia.

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
  • Affinity small molecules for the EPO receptor
  • Affinity small molecules for the EPO receptor
  • Affinity small molecules for the EPO receptor

Examples

Experimental program
Comparison scheme
Effect test

Embodiment Construction

[0139] The initial competitive ERP screening assay was designed as a solid plate binding assay. A detailed protocol of the assay is described below in the Protocolfor ERP Screen section.

[0140] Briefly, in the competitive ERP screening assay, the extracellular portion of EPO-R was purchased from R&D (Minneapolis, Minn.); biotinylated and regular peptide were synthesized by American Peptide Company; receptor and biotinylated peptide (bio-ERP) were incubated at room temperature; the solution was contacated with neutravidin (streptavidin) coated plate to bind any complex between receptor and peptide; the complex that was bound to the plate is detected by antibody specific for EPO-R and detection is performed with HRP-conjugated secondary antibody; the presence of the complex between receptor and peptide is detected by an light absorbance at 490 nm; and lack of or low signal indicates that the biotinylated peptide has been competed out, indicating an affinity of the test compound for the...

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

PropertyMeasurementUnit
Volumeaaaaaaaaaa
Volumeaaaaaaaaaa
Volumeaaaaaaaaaa
Login to View More

Abstract

Compounds are provided that complex with the modulating domain of erythropoietin receptor (EPO-R) for use with EPO-R to determine the presence of EPO-R, the ability of other molecules to bind to the modulating domain in competitive assays and to induce a signal by EPO-R into a cell when bound by the subject compounds in a physiological environment. The compounds are characterized by having a six-membered heterocyclic ring comprising at least one nitrogen atom and include substituted triazolopyrimidine, pyridazinone, pyridine and piperidine.

Description

[0001] This application is a continuation of provisional patent applications, Nos. 60 / 393,361; 60 / 393,360 and 60 / 394,110, all filed on Jul. 3, 2002, the entire contents of each of which is incorporated herein by reference.STATEMENT TO COMPUTER DISK AND SEQUENCE LISTING[0002] This application includes a sequence listing of 2 sequences and a computer disk labeled "Sequence Listing for application entitled "Affinity Small Molecules for the EPO Receptor" by Lennart Olsson and Tatjana Naranda" containing files "REC105-SEQLIST.prj" dated "Jul. 2, 2003" with 990 bytes, which is the PatentIn project file generated using PatentIn Version 3.0 software provided by the USPTO, and "REC105-SEQLIST.doc", dated "Jul. 2, 2003" with 21 kilobytes, which is the generated sequence listing from the PatentIn project file REC105-SEQLIST.prj using PatentIn Version 3.0 software, all which are herein incorporated. The information recorded in computer readable format on the incorporated computer disk labeled "...

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
IPC IPC(8): A61K31/519A61K38/17A61K45/06C07D487/04C07K14/71C12N5/07C12N5/071G01N33/566G01N33/74
CPCA61K31/519A61K38/17A61K45/06C07D487/04C07K14/71G01N33/566G01N2500/00G01N33/746A61K2300/00A61P7/06
Inventor OLSSON, LENNARTNARANDA, TATJANA
Owner F HOFFMANN LA ROCHE & CO AG
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