Issue 40, 2016

Artificial membranes with selective nanochannels for protein transport

Abstract

A poly(styrene-b-tert-butoxystyrene-b-styrene) copolymer was synthesized by anionic polymerization and hydrolyzed to poly(styrene-b-4-hydroxystyrene-b-styrene). Lamellar morphology was confirmed in the bulk after annealing. Membranes were fabricated by self-assembly of the hydrolyzed copolymer in solution, followed by water induced phase separation. A high density of pores of 4 to 5 nm diameter led to a water permeance of 40 L m−2 h−1 bar−1 and molecular weight cut-off around 8 kg mol−1. The morphology was controlled by tuning the polymer concentration, evaporation time, and the addition of imidazole and pyridine to stabilize the terpolymer micelles in the casting solution via hydrogen bond complexes. Transmission electron microscopy of the membrane cross-sections confirmed the formation of channels with hydroxyl groups beneficial for hydrogen-bond forming sites. The morphology evolution was investigated by time-resolved grazing incidence small angle X-ray scattering experiments. The membrane channels reject polyethylene glycol with a molecular size of 10 kg mol−1, but are permeable to proteins, such as lysozyme (14.3 kg mol−1) and cytochrome c (12.4 kg mol−1), due to the right balance of hydrogen bond interactions along the channels, electrostatic attraction, as well as the right pore sizes. Our results demonstrate that artificial channels can be designed for protein transport via block copolymer self-assembly using classical methods of membrane preparation.

Graphical abstract: Artificial membranes with selective nanochannels for protein transport

Article information

Article type
Paper
Submitted
11 Aug 2016
Accepted
04 Sep 2016
First published
05 Sep 2016

Polym. Chem., 2016,7, 6189-6201

Artificial membranes with selective nanochannels for protein transport

B. Sutisna, G. Polymeropoulos, E. Mygiakis, V. Musteata, K.-V. Peinemann, D.-M. Smilgies, N. Hadjichristidis and S. P. Nunes, Polym. Chem., 2016, 7, 6189 DOI: 10.1039/C6PY01401A

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