Disassembly of Dipeptide Single Crystals Can Transform the Lipid Membrane into a Network

Meifang Fu; Qi Li; Bingbing Sun; Yang Yang; Luru Dai; Tommy Nylander; Junbai Li

doi:10.1021/acsnano.7b03468

Disassembly of Dipeptide Single Crystals Can Transform the Lipid Membrane into a Network

Meifang Fu, Qi Li, Bingbing Sun, Yang Yang, Luru Dai, Tommy Nylander, Junbai Li

University of the Chinese Academy of Sciences

Research output: Contribution to journal › Article › peer-review

Abstract

Coupling between cytoskeleton and membranes is critical to cell movement as well as organelle formation. Here, we demonstrate that self-assembled single crystals of a dipeptide, diphenylalanine (FF), can interact with liposomes to form cytoskeleton-like structures. Under a physiological condition, disassembly of FF crystals deforms and translocates supported lipid membrane. The system exhibits similar dynamic characteristics to the endoplasmic reticulum (ER) network in cells. This bottom-up system thus indicates that external matter can participate in the deformation of liposomes, and disassembly of the nanostructures enables a system with distinct dynamic behaviors.

Original language	English
Pages (from-to)	7349-7354
Number of pages	6
Journal	ACS Nano
Volume	11
Issue number	7
DOIs	https://doi.org/10.1021/acsnano.7b03468
Publication status	Published - 2017 Jul 25

Subject classification (UKÄ)

Physical Chemistry (including Surface- and Colloid Chemistry)

Free keywords

biomimetic
membranes
peptides
phospholipids
self-assembly

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10.1021/acsnano.7b03468

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abstract = "Coupling between cytoskeleton and membranes is critical to cell movement as well as organelle formation. Here, we demonstrate that self-assembled single crystals of a dipeptide, diphenylalanine (FF), can interact with liposomes to form cytoskeleton-like structures. Under a physiological condition, disassembly of FF crystals deforms and translocates supported lipid membrane. The system exhibits similar dynamic characteristics to the endoplasmic reticulum (ER) network in cells. This bottom-up system thus indicates that external matter can participate in the deformation of liposomes, and disassembly of the nanostructures enables a system with distinct dynamic behaviors.",

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AU - Fu, Meifang

AU - Li, Qi

AU - Sun, Bingbing

AU - Yang, Yang

AU - Dai, Luru

AU - Nylander, Tommy

AU - Li, Junbai

PY - 2017/7/25

Y1 - 2017/7/25

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AB - Coupling between cytoskeleton and membranes is critical to cell movement as well as organelle formation. Here, we demonstrate that self-assembled single crystals of a dipeptide, diphenylalanine (FF), can interact with liposomes to form cytoskeleton-like structures. Under a physiological condition, disassembly of FF crystals deforms and translocates supported lipid membrane. The system exhibits similar dynamic characteristics to the endoplasmic reticulum (ER) network in cells. This bottom-up system thus indicates that external matter can participate in the deformation of liposomes, and disassembly of the nanostructures enables a system with distinct dynamic behaviors.

KW - biomimetic

KW - membranes

KW - peptides

KW - phospholipids

KW - self-assembly

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M3 - Article

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SN - 1936-0851

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JO - ACS Nano

JF - ACS Nano

IS - 7

ER -

Disassembly of Dipeptide Single Crystals Can Transform the Lipid Membrane into a Network

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Subject classification (UKÄ)

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