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Portrait of Tommy Nylander. Photo: Kennet Ruona

Tommy Nylander

Professor

Portrait of Tommy Nylander. Photo: Kennet Ruona

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

Author

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

Summary, in English

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.

Department/s

  • Physical Chemistry
  • NanoLund: Center for Nanoscience

Publishing year

2017-07-25

Language

English

Pages

7349-7354

Publication/Series

ACS Nano

Volume

11

Issue

7

Document type

Journal article

Publisher

The American Chemical Society (ACS)

Topic

  • Physical Chemistry

Keywords

  • biomimetic
  • membranes
  • peptides
  • phospholipids
  • self-assembly

Status

Published

ISBN/ISSN/Other

  • ISSN: 1936-0851