The European Physical Journal E

, Volume 4, Issue 4, pp 403–410

Amphiphilic block copolymer nanocontainers as bioreactors

  • C. Nardin
  • J. Widmer
  • M. Winterhalter
  • W. Meier

DOI: 10.1007/s101890170095

Cite this article as:
Nardin, C., Widmer, J., Winterhalter, M. et al. Eur. Phys. J. E (2001) 4: 403. doi:10.1007/s101890170095

Abstract:

Self-assembly of an amphiphilic triblock copolymer carrying polymerizable end-groups is used to prepare nanometer-sized vesicular structures in aqueous solution. The triblock copolymer shells of the vesicles can be regarded as a mimetic of biological membranes although they are 2 to 3 times thicker than a conventional lipid bilayer. Nevertheless, they can serve as a matrix for membrane-spanning proteins. Surprisingly, the proteins remain functional despite the extreme thickness of the membranes and that even after polymerization of the reactive triblock copolymers. This opens a new field to create mechanically stable protein/polymer hybrid membranes. As a representative example we functionalize (polymerized) triblock copolymer vesicles by reconstituting a channel-forming protein from the outer cell wall of Gram-negative bacteria. The protein used (OmpF) acts as a size-selective filter, which allows only for passage of molecules with a molecular weight below 400 g mol-1. Therefore substrates may still have access to enzymes encapsulated in such protein/polymer hybrid nanocontainers. We demonstrate this using the enzyme β-lactamase which is able to hydrolyze the antibiotic ampicillin. In addition, a transmembrane voltage above a given threshold causes a reversible gating transition of OmpF. This can be used to reversibly activate or deactivate the resulting nanoreactors.

PACS. 83.70.Hq Heterogeneous liquids: suspensions, dispersions, emulsions, pastes, slurries, foams, block copolymers, etc. – 81.05.Ys Nanophase materials – 87.68.+z Biomaterials and biological interfaces

Copyright information

© EDP Sciences, Springer-Verlag, Società Italiana di Fisica 2001

Authors and Affiliations

  • C. Nardin
    • 1
  • J. Widmer
    • 1
  • M. Winterhalter
    • 2
  • W. Meier
    • 1
  1. 1.Department of Physical Chemistry, University of Basel, Klingelbergstrasse 80, CH-4056 Basel, SwitzerlandCH
  2. 2.Institut de Pharmacologie et de Biologie Structurale, CNRS, 205 route de Narbonne, F-31077 Toulouse, FranceFR