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Multifunctional synthetic nano-chaperone for peptide folding and intracellular delivery

Author

Listed:
  • Il-Soo Park

    (Seoul National University)

  • Seongchan Kim

    (Korea Institute of Science and Technology (KIST))

  • Yeajee Yim

    (Seoul National University)

  • Ginam Park

    (Seoul National University)

  • Jinahn Choi

    (Seoul National University)

  • Cheolhee Won

    (Institute of Biotherapeutics Convergence Technology, Lemonex Inc)

  • Dal-Hee Min

    (Seoul National University
    Institute of Biotherapeutics Convergence Technology, Lemonex Inc)

Abstract

Artificial, synthetic chaperones have attracted much attention in biomedical research due to their ability to control the folding of proteins and peptides. Here, we report bio-inspired multifunctional porous nanoparticles to modulate proper folding and intracellular delivery of therapeutic α-helical peptide. The Synthetic Nano-Chaperone for Peptide (SNCP) based on porous nanoparticles provides an internal hydrophobic environment which contributes in stabilizing secondary structure of encapsulated α-helical peptides due to the hydrophobic internal environments. In addition, SNCP with optimized inner surface modification not only improves thermal stability for α-helical peptide but also supports the peptide stapling methods in situ, serving as a nanoreactor. Then, SNCP subsequently delivers the stabilized therapeutic α-helical peptides into cancer cells, resulting in high therapeutic efficacy. SNCP improves cellular uptake and bioavailability of the anti-cancer peptide, so the cancer growth is effectively inhibited in vivo. These data indicate that the bio-inspired SNCP system combining nanoreactor and delivery carrier could provide a strategy to expedite the development of peptide therapeutics by overcoming existing drawbacks of α-helical peptides as drug candidates.

Suggested Citation

  • Il-Soo Park & Seongchan Kim & Yeajee Yim & Ginam Park & Jinahn Choi & Cheolhee Won & Dal-Hee Min, 2022. "Multifunctional synthetic nano-chaperone for peptide folding and intracellular delivery," Nature Communications, Nature, vol. 13(1), pages 1-11, December.
  • Handle: RePEc:nat:natcom:v:13:y:2022:i:1:d:10.1038_s41467-022-32268-2
    DOI: 10.1038/s41467-022-32268-2
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    References listed on IDEAS

    as
    1. F. Ulrich Hartl & Andreas Bracher & Manajit Hayer-Hartl, 2011. "Molecular chaperones in protein folding and proteostasis," Nature, Nature, vol. 475(7356), pages 324-332, July.
    2. Dong Hoon Han & Hee-Kyung Na & Won Hoon Choi & Jung Hoon Lee & Yun Kyung Kim & Cheolhee Won & Seung-Han Lee & Kwang Pyo Kim & Jeff Kuret & Dal-Hee Min & Min Jae Lee, 2014. "Direct cellular delivery of human proteasomes to delay tau aggregation," Nature Communications, Nature, vol. 5(1), pages 1-8, December.
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