Mitochondria localization induced self-assembly of peptide amphiphiles for cellular dysfunction
Autor: | Eun Min Go, Huyeon Choi, Chaekyu Kim, M. T. Jeena, Eunji Lee, L. Palanikumar, Myoung Gyun Kang, Sung Chul Bae, Sang Kyu Kwak, Ja-Hyoung Ryu, Seon-Mi Jin, Sooham Park, Seonik Lee, Inhye Kim, Hyun-Woo Rhee |
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Jazyk: | angličtina |
Rok vydání: | 2017 |
Předmět: |
Science
General Physics and Astronomy Peptide Apoptosis 02 engineering and technology Mitochondrion Biology 010402 general chemistry 01 natural sciences General Biochemistry Genetics and Molecular Biology Article Cell Line chemistry.chemical_compound Mice Peptide amphiphile Moiety Animals Humans chemistry.chemical_classification Multidisciplinary Dipeptide Cell Death General Chemistry 021001 nanoscience & nanotechnology 0104 chemical sciences Transport protein Mitochondria Protein Transport chemistry Biochemistry Biophysics Mitochondrion localization 0210 nano-technology Peptides Reactive Oxygen Species Intracellular HeLa Cells |
Zdroj: | Nature Communications, Vol 8, Iss 1, Pp 1-10 (2017) Nature Communications NATURE COMMUNICATIONS(8) |
ISSN: | 2041-1723 |
Popis: | Achieving spatiotemporal control of molecular self-assembly associated with actuation of biological functions inside living cells remains a challenge owing to the complexity of the cellular environments and the lack of characterization tools. We present, for the first time, the organelle-localized self-assembly of a peptide amphiphile as a powerful strategy for controlling cellular fate. A phenylalanine dipeptide (FF) with a mitochondria-targeting moiety, triphenyl phosphonium (Mito-FF), preferentially accumulates inside mitochondria and reaches the critical aggregation concentration to form a fibrous nanostructure, which is monitored by confocal laser scanning microscopy and transmission electron microscopy. The Mito-FF fibrils induce mitochondrial dysfunction via membrane disruption to cause apoptosis. The organelle-specific supramolecular system provides a new opportunity for therapeutics and in-depth investigations of cellular functions. Spatiotemporal control of intracellular molecular self-assembly holds promise for therapeutic applications. Here the authors develop a peptide consisting of a phenylalanine dipeptide with a mitochondrial targeting moiety to form self-assembling fibrous nanostructures within mitochondria, leading to apoptosis. |
Databáze: | OpenAIRE |
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