한빛사 논문
Il-Soo Park1,4, Seongchan Kim2,4, Yeajee Yim1, Ginam Park1, Jinahn Choi1, Cheolhee Won3 & Dal-Hee Min1,3*
1Department of Chemistry, Seoul National University, Seoul 08826, Republic of Korea.
2Biomaterials Research Center, Biomedical Research Division, Korea Institute of Science and Technology (KIST), Seoul 02792, Republic of Korea.
3Institute of Biotherapeutics Convergence Technology, Lemonex Inc, Seoul 06683, Republic of Korea.
4These authors contributed equally: Il-Soo Park, Seongchan Kim.
*Corresponding author.
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 em>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.
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