Disassembly of Dipeptide Single Crystals Can Transform the Lipid Membrane into a Network
(2017) In ACS Nano 11(7). p.7349-7354- 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.
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/dd298d28-8a4f-49c9-9159-4a999a29f248
- author
- Fu, Meifang ; Li, Qi ; Sun, Bingbing ; Yang, Yang LU ; Dai, Luru ; Nylander, Tommy LU and Li, Junbai
- organization
- publishing date
- 2017-07-25
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- biomimetic, membranes, peptides, phospholipids, self-assembly
- in
- ACS Nano
- volume
- 11
- issue
- 7
- pages
- 6 pages
- publisher
- The American Chemical Society (ACS)
- external identifiers
-
- pmid:28657720
- wos:000406649700083
- scopus:85026300151
- ISSN
- 1936-0851
- DOI
- 10.1021/acsnano.7b03468
- language
- English
- LU publication?
- yes
- id
- dd298d28-8a4f-49c9-9159-4a999a29f248
- date added to LUP
- 2017-08-31 13:12:53
- date last changed
- 2024-04-14 16:43:40
@article{dd298d28-8a4f-49c9-9159-4a999a29f248, abstract = {{<p>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.</p>}}, author = {{Fu, Meifang and Li, Qi and Sun, Bingbing and Yang, Yang and Dai, Luru and Nylander, Tommy and Li, Junbai}}, issn = {{1936-0851}}, keywords = {{biomimetic; membranes; peptides; phospholipids; self-assembly}}, language = {{eng}}, month = {{07}}, number = {{7}}, pages = {{7349--7354}}, publisher = {{The American Chemical Society (ACS)}}, series = {{ACS Nano}}, title = {{Disassembly of Dipeptide Single Crystals Can Transform the Lipid Membrane into a Network}}, url = {{http://dx.doi.org/10.1021/acsnano.7b03468}}, doi = {{10.1021/acsnano.7b03468}}, volume = {{11}}, year = {{2017}}, }