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

ACS Nano. 2017 Jul 25;11(7):7349-7354. doi: 10.1021/acsnano.7b03468. Epub 2017 Jun 30.

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.

Keywords: biomimetic; membranes; peptides; phospholipids; self-assembly.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Biomimetic Materials / chemistry*
  • Crystallization
  • Cytoskeleton / chemistry
  • Dipeptides / chemistry*
  • Liposomes / chemistry*
  • Membrane Lipids / chemistry*
  • Nanostructures / chemistry*
  • Nanostructures / ultrastructure
  • Phenylalanine / analogs & derivatives*
  • Phenylalanine / chemistry

Substances

  • Dipeptides
  • Liposomes
  • Membrane Lipids
  • phenylalanylphenylalanine
  • Phenylalanine