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Area of Science:

  • Biotechnology
  • Nanotechnology
  • Molecular Biology

Background:

  • Bacterial inclusion bodies are nanoscale, functional protein amyloids capable of cell penetration.
  • Their therapeutic potential is limited by a lack of cell-specific targeting.
  • Targeted delivery is crucial for applications like protein replacement therapy.

Purpose of the Study:

  • To engineer bacterial inclusion bodies for specific cell targeting.
  • To assess the functionality of fused tumor-homing peptides (R9 and T22).
  • To confer CXCR4 specificity for enhanced cell binding and uptake.

Main Methods:

  • Genetic fusion of CXCR4-targeting peptides to a green fluorescent protein (GFP).
  • Production of fusion proteins in Escherichia coli.
  • Assessment of cell binding, penetration, and toxicity using specific inhibitors.

Main Results:

  • Engineered inclusion bodies were produced in full-length form with retained GFP fluorescence.
  • Fused peptides maintained their interaction potential and functionality.
  • Inclusion bodies demonstrated CXCR4-mediated, non-toxic penetration into CXCR4+ cells.

Conclusions:

  • Genetically targeted bacterial inclusion bodies can specifically bind and penetrate target cells.
  • This approach offers a cost-effective method for tissue-specific intracellular protein transfer.
  • Engineered inclusion bodies represent a promising platform for novel therapeutic delivery systems.