Issue 24, 2013
From the journal:

Journal of Materials Chemistry B

Nanoscale organization of proteinsviablock copolymerlithography and non-covalent bioconjugation†

Irene C. Reynhout,a   Guillaume Delaittre,bc   Ho-Cheol Kim,d   Roeland J. M. Nolte*a  and  Jeroen J. L. M. Cornelissen*e  

* Corresponding authors

a Radboud University Nijmegen, Institute for Molecules and Materials, Heyendaalseweg 135, Nijmegen, 6525 AJ, The Netherlands
E-mail: r.nolte@science.ru.nl
Fax: +31 (0)243653393
Tel: +31 (0)243652143

b Institute of Toxicology and Genetics, Karlsruhe Institute of Technology (KIT), Hermann-von-Helmholtz-Platz 1, Eggenstein-Leopoldshafen, 76344, Germany

c Preparative Macromolecular Chemistry, Institut für Technische und Polymerchemie, Karlsruhe Institute of Technology (KIT), Engesserstr. 18, 76128 Karlsruhe, Germany

d IBM Almaden Research Center, 650 Harry Road, San Jose, CA 95120, USA

e Laboratory for Biomolecular Nanotechnology, MESA+ Institute, University of Twente, PO Box 217, Enschede, 7500 AE, The Netherlands
E-mail: j.j.l.m.cornelissen@utwente.nl
Fax: +31 (0)534894645
Tel: +31 (0)534894380

Abstract

Thin films of cylinder-forming biotinylated poly(ethylene glycol)-polystyrene (PEG-b-PS) block copolymers were studied as a means to produce protein patterns. The orientation of the PEG cylinders depended on the end group functionality as well as on the preparation conditions. In the case of perpendicular cylinders, immobilization of single streptavidin molecules could be achieved. This immobilization was controlled by varying the amount of biotin in the films by mixing with non-functional PEG-b-PS.

Graphical abstract: Nanoscale organization of proteins via block copolymer lithography and non-covalent bioconjugation

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Article information

DOI
https://doi.org/10.1039/C3TB20411A
Article type
Communication
Submitted
24 mar 2013
Accepted
01 may 2013
First published
01 may 2013

J. Mater. Chem. B, 2013,1, 3026-3030

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Nanoscale organization of proteins via block copolymer lithography and non-covalent bioconjugation

I. C. Reynhout, G. Delaittre, H. Kim, R. J. M. Nolte and J. J. L. M. Cornelissen, J. Mater. Chem. B, 2013, 1, 3026 DOI: 10.1039/C3TB20411A

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