Mitochondria localization induced self-assembly of peptide amphiphiles for cellular dysfunction

Mitochondria localization induced self-assembly of peptide amphiphiles for cellular dysfunction

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 s...

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Published in:Nature communications Vol. 8; no. 1; p. 26
Main Authors: Jeena, M. T., Palanikumar, L., Go, Eun Min, Kim, Inhye, Kang, Myoung Gyun, Lee, Seonik, Park, Sooham, Choi, Huyeon, Kim, Chaekyu, Jin, Seon-Mi, Bae, Sung Chul, Rhee, Hyun Woo, Lee, Eunji, Kwak, Sang Kyu, Ryu, Ja-Hyoung
Format: Journal Article
Language:English
Published: London Nature Publishing Group UK 21-06-2017
Nature Portfolio
Subjects:
631/80/82/23
639/638/541/960
639/638/541/966
Animals
Apoptosis
Cell Death - physiology
Cell Line
HeLa Cells
Humanities and Social Sciences
Humans
Mice
Mitochondria - metabolism
multidisciplinary
Peptides - chemical synthesis
Peptides - genetics
Peptides - metabolism
Protein Transport
Reactive Oxygen Species
Science
Science (multidisciplinary)
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Summary: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.
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ISSN:2041-1723
2041-1723
DOI:10.1038/s41467-017-00047-z