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DC Field | Value | Language |
---|---|---|
dc.citation.endPage | 4813 | - |
dc.citation.number | 12 | - |
dc.citation.startPage | 4806 | - |
dc.citation.title | BIOMACROMOLECULES | - |
dc.citation.volume | 21 | - |
dc.contributor.author | Jin, Seongeon | - |
dc.contributor.author | Jeena, M. T. | - |
dc.contributor.author | Jana, Batakrishna | - |
dc.contributor.author | Moon, Minhyeok | - |
dc.contributor.author | Choi, Huyeon | - |
dc.contributor.author | Lee, Eunji | - |
dc.contributor.author | Ryu, Ja-Hyoung | - |
dc.date.accessioned | 2023-12-21T16:38:51Z | - |
dc.date.available | 2023-12-21T16:38:51Z | - |
dc.date.created | 2020-12-22 | - |
dc.date.issued | 2020-12 | - |
dc.description.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. | - |
dc.identifier.bibliographicCitation | BIOMACROMOLECULES, v.21, no.12, pp.4806 - 4813 | - |
dc.identifier.doi | 10.1021/acs.biomac.0c01000 | - |
dc.identifier.issn | 1525-7797 | - |
dc.identifier.scopusid | 2-s2.0-85098472066 | - |
dc.identifier.uri | https://scholarworks.unist.ac.kr/handle/201301/48992 | - |
dc.identifier.url | https://pubs.acs.org/doi/10.1021/acs.biomac.0c01000 | - |
dc.identifier.wosid | 000599993400014 | - |
dc.language | 영어 | - |
dc.publisher | AMER CHEMICAL SOC | - |
dc.title | Spatiotemporal Self-Assembly of Peptides Dictates Cancer-Selective Toxicity | - |
dc.type | Article | - |
dc.description.isOpenAccess | FALSE | - |
dc.relation.journalWebOfScienceCategory | Biochemistry & Molecular Biology; Chemistry, Organic; Polymer Science | - |
dc.relation.journalResearchArea | Biochemistry & Molecular Biology; Chemistry; Polymer Science | - |
dc.type.docType | Article | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.subject.keywordPlus | NILE RED | - |
dc.subject.keywordPlus | MITOCHONDRIA | - |
dc.subject.keywordPlus | APOPTOSIS | - |
dc.subject.keywordPlus | HYDROPHOBICITY | - |
dc.subject.keywordPlus | SURFACTANT | - |
dc.subject.keywordPlus | CELLS | - |
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