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Ryu, Ja-Hyoung
Supramolecular NanoMaterials Lab (SUN)
Research Interests
  • Supramolecular assembly, synthetic peptide assembly, cancer drug delivery

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Spatiotemporal Self-Assembly of Peptides Dictates Cancer-Selective Toxicity

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Title
Spatiotemporal Self-Assembly of Peptides Dictates Cancer-Selective Toxicity
Author
Jin, SeongeonJeena, M. T.Jana, BatakrishnaMoon, MinhyeokChoi, HuyeonLee, EunjiRyu, Ja-Hyoung
Issue Date
2020-12
Publisher
AMER CHEMICAL SOC
Citation
BIOMACROMOLECULES, v.21, no.12, pp.4806 - 4813
Abstract
The intracellular or pericellular self-assembly of amphiphilic peptides is emerging as a potent cancer therapeutic strategy. Achieving the self-assembly of amphiphilic peptides inside a cell or cellular organelle is challenging due to the complex cellular environment, which consists of many amphiphilic biomolecules that may alter the self-assembling propensity of the synthetic peptides. Herein, we show that the hydrophobic-hydrophilic balance of the amphiphilic peptides determines the self-assembling propensity, thereby controlling the fate of the cell. A series of peptides were designed to target and self-assemble inside the mitochondria of cancer cells. The hydrophobicity of the peptides was tuned by varying their N-terminus capping. The analysis showed that the largest hydrophobic peptide was self-assembled before reaching the mitochondria and showed no selectivity toward cancer cells, whereas hydrophilic peptides could not self-assemble inside the mitochondria. Optimum balance between hydrophobicity and hydrophilicity is a critical factor for achieving self-assembly inside the mitochondria, thereby providing greater selectivity against cancer cells.
URI
https://scholarworks.unist.ac.kr/handle/201301/48992
URL
https://pubs.acs.org/doi/10.1021/acs.biomac.0c01000
DOI
10.1021/acs.biomac.0c01000
ISSN
1525-7797
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CHM_Journal Papers
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