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

Autor:	Jeena MT; Department of Chemistry, Ulsan National Institute of Science and Technology (UNIST), Ulsan, 44919, Republic of Korea., Palanikumar L; Department of Chemistry, Ulsan National Institute of Science and Technology (UNIST), Ulsan, 44919, Republic of Korea., Go EM; School of Energy and Chemical Engineering, Ulsan National Institute of Science and Technology (UNIST), Ulsan, 44919, Republic of Korea., Kim I; Graduate School of Analytical Science and Technology, Chungnam National University, Daejeon, 34134, Republic of Korea., Kang MG; Department of Chemistry, Ulsan National Institute of Science and Technology (UNIST), Ulsan, 44919, Republic of Korea., Lee S; Department of Biological Engineering, Ulsan National Institute of Science and Technology (UNIST), Ulsan, 44919, Republic of Korea., Park S; Department of Chemistry, Ulsan National Institute of Science and Technology (UNIST), Ulsan, 44919, Republic of Korea., Choi H; Department of Chemistry, Ulsan National Institute of Science and Technology (UNIST), Ulsan, 44919, Republic of Korea., Kim C; Department of Chemistry, Ulsan National Institute of Science and Technology (UNIST), Ulsan, 44919, Republic of Korea., Jin SM; Graduate School of Analytical Science and Technology, Chungnam National University, Daejeon, 34134, Republic of Korea., Bae SC; Department of Biological Engineering, Ulsan National Institute of Science and Technology (UNIST), Ulsan, 44919, Republic of Korea., Rhee HW; Department of Chemistry, Ulsan National Institute of Science and Technology (UNIST), Ulsan, 44919, Republic of Korea., Lee E; Graduate School of Analytical Science and Technology, Chungnam National University, Daejeon, 34134, Republic of Korea. eunjilee@cnu.ac.kr., Kwak SK; School of Energy and Chemical Engineering, Ulsan National Institute of Science and Technology (UNIST), Ulsan, 44919, Republic of Korea. skkwak@unist.ac.kr., Ryu JH; Department of Chemistry, Ulsan National Institute of Science and Technology (UNIST), Ulsan, 44919, Republic of Korea. jhryu@unist.ac.kr.
Jazyk:	angličtina
Zdroj:	Nature communications [Nat Commun] 2017 Jun 21; Vol. 8 (1), pp. 26. Date of Electronic Publication: 2017 Jun 21.
DOI:	10.1038/s41467-017-00047-z
Abstrakt:	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:	MEDLINE
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