IDEAS home Printed from https://ideas.repec.org/a/nat/natcom/v13y2022i1d10.1038_s41467-022-32268-2.html
   My bibliography  Save this article

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
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/s41467-022-32268-2
    File Function: Abstract
    Download Restriction: no
    File URL: https://libkey.io/10.1038/s41467-022-32268-2?utm_source=ideas
    LibKey link: if access is restricted and if your library uses this service, LibKey will redirect you to where you can use your library subscription to access this item
    ---><---

    References listed on IDEAS

    as
    1. 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.
    2. 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.
    Full references (including those not matched with items on IDEAS)

    Most related items

    These are the items that most often cite the same works as this one and are cited by the same works as this one.
    1. Erik B Nordquist & Charles A English & Eugenia M Clerico & Woody Sherman & Lila M Gierasch & Jianhan Chen, 2021. "Physics-based modeling provides predictive understanding of selectively promiscuous substrate binding by Hsp70 chaperones," PLOS Computational Biology, Public Library of Science, vol. 17(11), pages 1-24, November.
    2. Franke, R., 2016. "CHIMERA: Top-down model for hierarchical, overlapping and directed cluster structures in directed and weighted complex networks," Physica A: Statistical Mechanics and its Applications, Elsevier, vol. 461(C), pages 384-408.
    3. Verena Kohler & Andreas Kohler & Lisa Larsson Berglund & Xinxin Hao & Sarah Gersing & Axel Imhof & Thomas Nyström & Johanna L. Höög & Martin Ott & Claes Andréasson & Sabrina Büttner, 2024. "Nuclear Hsp104 safeguards the dormant translation machinery during quiescence," Nature Communications, Nature, vol. 15(1), pages 1-20, December.
    4. Matthias M. Schneider & Saurabh Gautam & Therese W. Herling & Ewa Andrzejewska & Georg Krainer & Alyssa M. Miller & Victoria A. Trinkaus & Quentin A. E. Peter & Francesco Simone Ruggeri & Michele Vend, 2021. "The Hsc70 disaggregation machinery removes monomer units directly from α-synuclein fibril ends," Nature Communications, Nature, vol. 12(1), pages 1-11, December.
    5. Maru Jaime-Garza & Carlos A. Nowotny & Daniel Coutandin & Feng Wang & Mariano Tabios & David A. Agard, 2023. "Hsp90 provides a platform for kinase dephosphorylation by PP5," Nature Communications, Nature, vol. 14(1), pages 1-12, December.
    6. Krishna B. S. Swamy & Hsin-Yi Lee & Carmina Ladra & Chien-Fu Jeff Liu & Jung-Chi Chao & Yi-Yun Chen & Jun-Yi Leu, 2022. "Proteotoxicity caused by perturbed protein complexes underlies hybrid incompatibility in yeast," Nature Communications, Nature, vol. 13(1), pages 1-14, December.
    7. Jaime Carrasco & Rosa Antón & Alejandro Valbuena & David Pantoja-Uceda & Mayur Mukhi & Rubén Hervás & Douglas V. Laurents & María Gasset & Javier Oroz, 2023. "Metamorphism in TDP-43 prion-like domain determines chaperone recognition," Nature Communications, Nature, vol. 14(1), pages 1-15, December.
    8. Martin Grønbæk-Thygesen & Vasileios Voutsinos & Kristoffer E. Johansson & Thea K. Schulze & Matteo Cagiada & Line Pedersen & Lene Clausen & Snehal Nariya & Rachel L. Powell & Amelie Stein & Douglas M., 2024. "Deep mutational scanning reveals a correlation between degradation and toxicity of thousands of aspartoacylase variants," Nature Communications, Nature, vol. 15(1), pages 1-18, December.
    9. Pengfei Xu & Joy C. Yang & Bo Chen & Shu Ning & Xiong Zhang & Leyi Wang & Christopher Nip & Yuqiu Shen & Oleta T. Johnson & Gabriela Grigorean & Brett Phinney & Liangren Liu & Qiang Wei & Eva Corey & , 2024. "Proteostasis perturbation of N-Myc leveraging HSP70 mediated protein turnover improves treatment of neuroendocrine prostate cancer," Nature Communications, Nature, vol. 15(1), pages 1-20, December.
    10. Emelie E. Aspholm & Jens Lidman & Björn M. Burmann, 2024. "Structural basis of substrate recognition and allosteric activation of the proapoptotic mitochondrial HtrA2 protease," Nature Communications, Nature, vol. 15(1), pages 1-18, December.
    11. Hyunju Cho & Yumeng Liu & SangYoon Chung & Sowmya Chandrasekar & Shimon Weiss & Shu-ou Shan, 2024. "Dynamic stability of Sgt2 enables selective and privileged client handover in a chaperone triad," Nature Communications, Nature, vol. 15(1), pages 1-16, December.
    12. Dahai Yu & Lin Lv & Li Fang & Bo Zhang & Junnan Wang & Ge Zhan & Lei Zhao & Xin Zhao & Baoxin Li, 2017. "Inhibitory effects and mechanism of dihydroberberine on hERG channels expressed in HEK293 cells," PLOS ONE, Public Library of Science, vol. 12(8), pages 1-19, August.
    13. Guosheng Chen & Linjing Tong & Siming Huang & Shuyao Huang & Fang Zhu & Gangfeng Ouyang, 2022. "Hydrogen-bonded organic framework biomimetic entrapment allowing non-native biocatalytic activity in enzyme," Nature Communications, Nature, vol. 13(1), pages 1-10, December.
    14. Verena Rukes & Mathieu E. Rebeaud & Louis W. Perrin & Paolo De Los Rios & Chan Cao, 2024. "Single-molecule evidence of Entropic Pulling by Hsp70 chaperones," Nature Communications, Nature, vol. 15(1), pages 1-8, December.
    15. Ke Shui & Chenwei Wang & Xuedi Zhang & Shanshan Ma & Qinyu Li & Wanshan Ning & Weizhi Zhang & Miaomiao Chen & Di Peng & Hui Hu & Zheng Fang & Anyuan Guo & Guanjun Gao & Mingliang Ye & Luoying Zhang & , 2023. "Small-sample learning reveals propionylation in determining global protein homeostasis," Nature Communications, Nature, vol. 14(1), pages 1-23, December.

    More about this item

    Statistics

    Access and download statistics

    Corrections

    All material on this site has been provided by the respective publishers and authors. You can help correct errors and omissions. When requesting a correction, please mention this item's handle: RePEc:nat:natcom:v:13:y:2022:i:1:d:10.1038_s41467-022-32268-2. See general information about how to correct material in RePEc.

    If you have authored this item and are not yet registered with RePEc, we encourage you to do it here. This allows to link your profile to this item. It also allows you to accept potential citations to this item that we are uncertain about.

    If CitEc recognized a bibliographic reference but did not link an item in RePEc to it, you can help with this form .

    If you know of missing items citing this one, you can help us creating those links by adding the relevant references in the same way as above, for each refering item. If you are a registered author of this item, you may also want to check the "citations" tab in your RePEc Author Service profile, as there may be some citations waiting for confirmation.

    For technical questions regarding this item, or to correct its authors, title, abstract, bibliographic or download information, contact: Sonal Shukla or Springer Nature Abstracting and Indexing (email available below). General contact details of provider: http://www.nature.com .

    Please note that corrections may take a couple of weeks to filter through the various RePEc services.

    IDEAS is a RePEc service. RePEc uses bibliographic data supplied by the respective publishers.