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Optical Tweezers to Study RNA-Protein Interactions in Translation Regulation
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Optical Tweezers to Study RNA-Protein Interactions in Translation Regulation

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Spatiotemporally Controllable Covalent Bonding of RNA for Multi-Protein Interference

Hao Fang1, Tingting Wang1, Jun Dai2

  • 1State Key Laboratory of Biogeology and Environmental Geology, Faculty of Materials Science and Chemistry, China University of Geosciences, Wuhan, 430074, China.

Advanced Healthcare Materials
|July 9, 2024
PubMed

Insights

Researchers developed PRFK, a novel dye-peptide conjugate that selectively targets and inhibits multiple protein synthesis in cancer cells. This photodynamic therapy approach offers improved spatiotemporal control for potential oncological treatments.

Area of Science:

  • Biomedical Engineering
  • Molecular Biology
  • Cancer Research

Background:

  • Genetic mutations and aberrant protein expression are hallmarks of diseases like cancer.
  • Targeting multiple protein synthesis pathways offers a promising therapeutic strategy for oncological diseases.
  • Existing multi-protein synthesis regulators lack precise spatiotemporal control and stability.

Purpose of the Study:

  • To develop a novel dye-peptide conjugate, PRFK, for targeted multi-protein interference with spatiotemporal selectivity and stability.
  • To investigate the mechanism of PRFK-mediated protein synthesis inhibition.
  • To evaluate the therapeutic potential of PRFK in a cancer cell model.

Main Methods:

  • Design and synthesis of the PRFK dye-peptide conjugate.
  • Utilizing a tumor-targeting peptide for cellular uptake and KDEL receptor (KDELR) binding in the endoplasmic reticulum (ER).
  • Employing light-activated photodynamic therapy to generate singlet oxygen (1O2) and create a cytidine-reactive intermediate.
  • Covalent binding of the intermediate to mRNA to inhibit protein synthesis.
  • Proteomic analysis of treated 4T1 cells to assess cellular pathway alterations.

Main Results:

  • PRFK demonstrated efficient uptake and specific binding to KDELR in tumor cells.
  • Light irradiation triggered 1O2 generation and subsequent mRNA targeting, blocking protein synthesis.
  • Proteomics data revealed significant alterations in apoptosis, ferroptosis, proliferation, migration, invasion, and immune infiltration pathways in 4T1 cells.
  • PRFK effectively disrupted cellular physiological activities, leading to tumor treatment outcomes.

Conclusions:

  • PRFK serves as a potent multi-protein interference probe with enhanced spatiotemporal selectivity and stability.
  • The study validates multi-protein interference as a viable strategy for cancer therapy.
  • PRFK holds potential for targeting protein synthesis in various subcellular organelles for future therapeutic applications.
Keywords:
aggregation‐induced emissioncovalent reactionmulti‐protein interferencephoto‐crosslinking probe

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