Mimicking multipass transmembrane proteins: synthesis, assembly and folding of alternating amphiphilic multiblock molecules in liposomal membranes

Chem Commun (Camb). 2011 Jan 7;47(1):194-6. doi: 10.1039/c0cc02420a. Epub 2010 Sep 17.

Abstract

Alternating amphiphilic multiblock molecules 1-4, involving fluorescent hydrophobic units, were designed as mimics for multipass transmembrane proteins. Fluorescence spectroscopy of 1-4 in liposomal membranes suggested the face-to-face stacking of the hydrophobic units to give folded structures as well as intermolecular assemblies.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Benzene Derivatives / chemical synthesis*
  • Benzene Derivatives / chemistry*
  • Liposomes / chemistry*
  • Membrane Proteins / chemistry*
  • Membranes, Artificial*
  • Molecular Mimicry*
  • Molecular Structure
  • Protein Folding
  • Spectrometry, Fluorescence

Substances

  • Benzene Derivatives
  • Liposomes
  • Membrane Proteins
  • Membranes, Artificial