
Tommy Nylander
Professor

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