Letter abstract
Nature Nanotechnology 2, 226 - 229 (2006)
Published online: 25 March 2007 | doi:10.1038/nnano.2007.76
Subject Categories: Molecular self-assembly | Nanobiotechnology
A virus-based biocatalyst
Noëlle Carette1, Hans Engelkamp2, Eric Akpa2, Sebastien J. Pierre3, Neil R. Cameron4, Peter C. M. Christianen2, Jan C. Maan2, Jens C. Thies3, Ralf Weberskirch5, Alan E. Rowan2, Roeland J. M. Nolte2, Thierry Michon1 & Jan C. M. Van Hest2
Abstract
Virus particles are probably the most precisely defined nanometre-sized objects that can be formed by protein self-assembly. Although their natural function is the storage and transport of genetic material, they have more recently been applied as scaffolds for mineralization and as containers for the encapsulation of inorganic compounds1, 2. The reproductive power of viruses has been used to develop versatile analytical methods, such as phage display, for the selection and identification of (bio)active compounds3. To date, the combined use of self-assembly and reproduction has not been used for the construction of catalytic systems. Here we describe a self-assembled system based on a plant virus that has its coat protein genetically modified to provide it with a lipase enzyme. Using single-object and bulk catalytic studies, we prove that the virus-anchored lipase molecules are catalytically active. This anchored biocatalyst, unlike man-made supported catalysts, has the capability to reproduce itself in vivo, generating many independent catalytically active copies.
- Interactions Plante Virus, UMR GDPP, IBVM, INRA, BP 81, F-33883, Villenave d'Ornon, France
- Institute for Molecules and Materials, Radboud University Nijmegen, PO Box 9010, 6500 GL, Nijmegen, The Netherlands
- DSM Research, PO Box 18, 6160 MD, Geleen, The Netherlands
- University of Durham, Department of Chemistry, South Road, Durham DH1 3LE, UK
- Technische Universität München, Chemie Department, Lehrstuhl für Makromolekulare Stoffe, Lichtenbergstrasse 4, 85747 Garching, Germany
Correspondence to: Thierry Michon1 e-mail: michon@bordeaux.inra.fr
Correspondence to: Jan C. M. Van Hest2 e-mail: j.vanhest@science.ru.nl
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