Unlock instant, AI-driven research and patent intelligence for your innovation.

Therapeutic sall4 peptide

一种中性、非极性的技术,应用在表达,4的,分离的肽接领域,能够解决缺乏靶标特异性等问题

Active Publication Date: 2019-06-07
NAT UNIV OF SINGAPORE +2
View PDF7 Cites 0 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

The main limitation of this peptide-based therapy is the lack of target specificity

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
  • Therapeutic sall4 peptide
  • Therapeutic sall4 peptide
  • Therapeutic sall4 peptide

Examples

Experimental program
Comparison scheme
Effect test

Embodiment

[0085] SALL4 binds to RBBp4 of NuRD

[0086] It was previously reported that SALL4WT binds to the NURD complex and blocks the SALL4-NuRD interaction. The histone-binding protein RBBp4 was hypothesized to be the SALL4-binding subunit in NuRD. To confirm the direct binding of SALL4 to RBBp4, a binding assay was performed using the 12 amino acid WT SALL4T (Figure 1). Using isothermal titration calorimetry, a direct interaction between SALL4 and the RBBp4 subunit of the NURD complex was demonstrated. The 12-aa SALL4 peptide binds to the K of RBBp4 D 1.04±0.06μM ( Figure 1A ). The binding kinetics were further confirmed using surface plasmon resonance, where the binding K between the SALL4 peptide and RBBp4 D Calculated to be 1.5 μM (k on =16830±460M -1 the s -1 ;k off=0.026±0.00045s -1 )( Figure 1B ). These results demonstrate that SALL4 directly binds to the NuRD complex through the NuRD subunit RBBp4.

[0087] Crystal structure of the RBBp4-SALL4 complex

[0088]...

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 provides, in certain embodiments, isolated peptides and pharmaceutical compositions comprising isolated peptides that bind to retinoblastoma binding protein 4 RBBp4 such that, the binding blocks the SALL4-RBBp4 interaction. Methods of inhibiting binding of SALL4 with RBBp4 and methods for treating a subject having a disorder mediated by a dysregulation of SALL4 are also provided.

Description

[0001] related application [0002] This application claims the benefit of US Provisional Application 62 / 329,010, filed April 28, 2016. The entire teaching of this application is incorporated herein by reference. [0003] Cite material incorporated into an ASCII text file [0004] This application incorporates by reference the Sequence Listing contained in the following ASCII text file filed concurrently herewith: [0005] a) File name: 44591138001_SEQUENCELISTING.txt, created on April 28, 2017, 13KB in size. Background technique [0006] Spalt-like transcription factor 4 (SALL4) has an integral role in developmental events and maintenance of stem cell pluripotency. SALL4 is a zinc finger transcription factor that, together with POU5FI (Oct4), Nanog and Sox2, forms a core transcriptional network that activates genes associated with the proliferation of embryonic stem cells (ESCs). SALL4 binds to retinoblastoma-binding protein 4 (RBBp4, which is a subunit of the nucleosome ...

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): A61K38/04A61K38/10A61K38/17C07K7/00C07K7/02C07K7/04C07K7/06
CPCA61K38/00C07K7/06C07K7/08C07K2319/033
Inventor 刘美慧D·G·特恩柴立谢青山A·波尔森
Owner NAT UNIV OF SINGAPORE
Features
  • R&D
  • Intellectual Property
  • Life Sciences
  • Materials
  • Tech Scout
Why Patsnap Eureka
  • Unparalleled Data Quality
  • Higher Quality Content
  • 60% Fewer Hallucinations
Social media
Patsnap Eureka Blog
Learn More