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Polyarginine and its analogues inhibit p53 mutant aggregation and cancer cell proliferation in vitro

Zhaolin Chen1, Jun Chen2, Venkateshwar G Keshamouni2

  • 1University of Michigan-Dearborn, Department of Mechanical Engineering, 4901 Evergreen Road, Dearborn, MI 48128, USA.

Biochemical and Biophysical Research Communications
|May 25, 2017
PubMed

Insights

Polyarginine and polyornithine show promise in inhibiting the aggregation of the tumor suppressor protein p53 (mutated) and reducing cancer cell growth. These findings suggest potential therapeutic applications for protein aggregation diseases.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Oncology

Background:

  • Arginine stabilizes proteins and corrects folding, making it a potential therapeutic for protein aggregation diseases.
  • Mutated tumor suppressor protein p53 aggregation is linked to tumor progression and uncontrolled cell growth.
  • Investigating arginine analogues for therapeutic potential against p53-related cancers.

Purpose of the Study:

  • To evaluate the inhibitory effects of polyarginine and its analogues on p53 mutant peptide aggregation.
  • To assess the impact of these compounds on p53 mutant cancer cell proliferation in vitro.
  • To explore potential therapeutic strategies for cancers driven by p53 aggregation.

Main Methods:

  • Biochemical assays were employed to measure peptide aggregation inhibition.
  • In vitro cell toxicity studies were conducted to assess compound effects on cancer cells.
  • Polyarginine, polyornithine, canavanine, and citrulline were tested as inhibitors.

Main Results:

  • Polyarginine and polyornithine significantly inhibited p53 conserved peptide aggregation at micromolar concentrations.
  • These compounds also demonstrated significant inhibition of p53 mutant cancer cell proliferation.
  • Canavanine and citrulline effects were also characterized.

Conclusions:

  • Polyarginine and polyornithine are effective inhibitors of p53 mutant peptide aggregation.
  • These compounds show potential as therapeutic agents for cancers associated with p53 mutations and aggregation.
  • Further research is warranted to explore their clinical applicability.
Keywords:
ArginineCancerCell proliferationInhibitionp53 aggregation

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