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

Beta-catenin targeting peptides and uses thereof

a technology of beta-catenin and peptides, which is applied in the direction of peptide/protein ingredients, peptide sources, drug compositions, etc., can solve the problems of lack of binding affinity and/or specificity, poor cell permeability, etc., and achieve the effect of increasing the helical character of peptides

Inactive Publication Date: 2015-10-08
PRESIDENT & FELLOWS OF HARVARD COLLEGE
View PDF15 Cites 31 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Benefits of technology

The patent describes a method called "peptide stapling" which involves creating a strong bond between two parts of a peptide using a hydrocarbon cross-linker generated through an olefin metathesis reaction. This stapling process helps maintain the peptide's native conformation and can lead to the creation of more stable and alpha-helical peptides. The technique can be used to modify peptides for various applications such as drug development.

Problems solved by technology

Small peptides usually exhibit little or no secondary structure when excised from the stabilizing protein context thereby becoming subjected to rapid degradation by proteases under physiological conditions, displaying poor cell permeability, and exhibiting a lack of binding affinity and / or specificity resulting from conformational flexibility.

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
  • Beta-catenin targeting peptides and uses thereof
  • Beta-catenin targeting peptides and uses thereof
  • Beta-catenin targeting peptides and uses thereof

Examples

Experimental program
Comparison scheme
Effect test

examples

[0405]Deregulation of Wnt / β-catenin signaling is associated with several types of cancer.

[0406]Especially, a reduced ability to degrade β-catenin, e.g., by the inactivation of the destruction complex or by loss of β-catenin phosphorylation sites, can be involved in the formation of cancer.[2, 3] Restoring this ability would contribute to target cancers that depend on deregulated Wnt signaling to grow. The manipulation of requisite protein-protein interactions offers a strategy to interfere with this pathway, e.g., targeting the signaling cascade downstream by inhibiting the interaction of β-catenin with TCF transcription factors (FIG. 2). This setup may allow for inhibition of Wnt signaling independent of the site of deregulation within the pathway.

[0407]Due to large interaction areas, the precise manipulation of protein-protein interactions is complicated.[6] In principle, an isolated bioactive helix of a protein could be used to interfere with such interactions. However, small pep...

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 relates to β-catenin targeting peptides comprising an α-helical segment that are optionally stapled or stitched, and pharmaceutical compositions thereof. Uses of the inventive β-catenin targeting polypeptides including methods for treatment of disease, such as diseases associated with aberrant Wnt signaling, including cancer, are also provided.

Description

RELATED APPLICATIONS[0001]The present application is a continuation of and claims priority under 35 U.S.C. §120 to U.S. Application, U.S. Ser. No. 13 / 825,709, filed Jun. 10, 2013, which is a national stage filing under 35 U.S.C. §371 of international PCT application, PCT / US2011 / 052755, filed Sep. 22, 2011, which claims priority under 35 U.S.C. §119(e) to U.S. provisional patent application, U.S. Ser. No. 61 / 385,405, filed Sep. 22, 2010, each of which is incorporated herein by reference.BACKGROUND OF THE INVENTION[0002]The WNT (Wingless and INT-1) signal transduction cascade is mediated by Wnt proteins and is involved in cell survival and proliferation as well as cell fate and movement.[1, 2] In the absence of Wnt proteins the transcriptional regulator β-catenin is recruited into a destruction complex that contains Adenomatous Polyposis Coli (APC) and Axin (FIG. 1a). This event facilitates the phosphorylation of β-catenin by casein kinase 1 (CK1) and glycogen synthase kinase-3β (GSK-...

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(United States)
IPC IPC(8): C07K14/47
CPCC07K14/4705A61K38/00C07K14/4702C07K14/47C07K14/4703C07K1/113C07K7/08
Inventor VERDINE, GREGORY L.GROSSMANN, TOM N.YEH, TSUNG-HAN JOHANNES
Owner PRESIDENT & FELLOWS OF HARVARD COLLEGE
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

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

© 2024 PatSnap. All rights reserved.Legal|Privacy policy|Modern Slavery Act Transparency Statement|Sitemap|About US| Contact US: help@patsnap.com