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

被引:32
作者
Fu, Meifang [1 ,3 ]
Li, Qi [1 ,3 ]
Sun, Bingbing [1 ,3 ]
Yang, Yang [2 ]
Dai, Luru [2 ]
Nylander, Tommy [4 ]
Li, Junbai [1 ,3 ]
机构
[1] Chinese Acad Sci, Inst Chem, CAS Key Lab Colloid Interface & Thermodynam, Beijing Natl Lab Mol Sci, Beijing 100190, Peoples R China
[2] Natl Ctr Nanosci & Technol, CAS Key Lab Biomed Effects Nanomat & Nanosafety, Beijing 100190, Peoples R China
[3] Univ Chinese Acad Sci, Beijing 100049, Peoples R China
[4] Lund Univ, Dept Chem, Div Phys Chem, POB 124, SE-22100 Lund, Sweden
基金
中国国家自然科学基金;
关键词
phospholipids; self-assembly; peptides; membranes; biomimetic; ASSEMBLED PEPTIDE NANOTUBES; CYTOSKELETON ADHESION; ENDOPLASMIC-RETICULUM; IN-VITRO; VESICLE; DIPHENYLALANINE; DYNAMICS; NANOSTRUCTURES; CONSTRUCTION; BIOLOGY;
D O I
10.1021/acsnano.7b03468
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
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.
引用
收藏
页码:7349 / 7354
页数:6
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