Inhibition of Retinoblastoma Protein Inactivation

Abstract

The objective of this project is to discover and characterize molecules that inhibit breast cancer cell proliferation by maintaining activity of the retinoblastoma protein (Rb). Rb is inactivated to drive proliferation in normal and cancer cells by phosphorylation, which dissociates the E2F transcription factor from Rb to activate S phase genes. Our goal is to find and characterize molecules that stabilize the complex between phosphorylated Rb and E2F. During the project period, we tested our proposed mechanism for how molecules may enhance the affinity of phosphorylated Rb (phosRb) for E2F by disrupting the compact phosRb conformation. We identified a proof-of-concept peptide that increases phosRb-affinity, we developed a fluorescence-based assay to identify small molecule enhancers of phos-Rb affinity, we performed a high throughput screen and further tested hits in the primary screen, and we began pursuing additional fragment-based approaches to identifying lead compounds.

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Document Details

Document Type
Technical Report
Publication Date
Nov 01, 2017
Accession Number
AD1048000

Entities

People

  • Seth M. Rubin

Organizations

  • University of California, Santa Cruz

Tags

DTIC Thesaurus Topics

  • Breast Cancer
  • Cell Physiological Processes
  • Chemistry
  • Electron Density
  • Electrons
  • Fluorescence
  • Lead Compounds
  • Mass Spectrometry
  • Molecules
  • Neoplasms
  • Papillomavirus Infections
  • Phosphorylation
  • Protein-Protein Interactions
  • Proteins
  • Retinal Diseases
  • Small Molecules
  • Transcription Factors

Fields of Study

  • Biology

Readers

  • Molecular Biology and Genetics
  • Molecular and Cellular Biochemistry