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
Jazyk: angličtina
Rok vydání: 2017
Předmět:
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