Letter abstract


Nature Nanotechnology 2, 635 - 639 (2007)
Published online: 23 September 2007 | doi:10.1038/nnano.2007.299

Subject Category: Nanobiotechnology

A virus-based single-enzyme nanoreactor

Marta Comellas-Aragonès1, Hans Engelkamp1, Victor I. Claessen1, Nico A. J. M. Sommerdijk2, Alan E. Rowan1, Peter C. M. Christianen1, Jan C. Maan1, Benedictus J. M. Verduin3, Jeroen J. L. M. Cornelissen1 & Roeland J. M. Nolte1


Most enzyme studies are carried out in bulk aqueous solution, at the so-called ensemble level, but more recently studies have appeared in which enzyme activity is measured at the level of a single molecule, revealing previously unseen properties1, 2, 3, 4. To this end, enzymes have been chemically or physically anchored to a surface, which is often disadvantageous because it may lead to denaturation. In a natural environment, enzymes are present in a confined reaction space, which inspired us to develop a generic method to carry out single-enzyme experiments in the restricted spatial environment of a virus capsid. We report here the incorporation of individual horseradish peroxidase enzymes in the inner cavity of a virus, and describe single-molecule studies on their enzymatic behaviour. These show that the virus capsid is permeable for substrate and product and that this permeability can be altered by changing pH.

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  1. Institute for Molecules and Materials, Radboud University Nijmegen, Toernooiveld 1, 6525 ED Nijmegen, The Netherlands
  2. Laboratory of Macromolecular and Organic Chemistry and Soft Matter CryoTEM Research Unit, Department of Biomedical Engineering, Eindhoven University of Technology, PO Box 513, 5600 MB, Eindhoven, The Netherlands
  3. Laboratory of Virology, Wageningen University, Binnenhaven 11, 6709 PD Wageningen, The Netherlands

Correspondence to: Hans Engelkamp1 e-mail: h.engelkamp@science.ru.nl

Correspondence to: Jeroen J. L. M. Cornelissen1 e-mail: j.cornelissen@science.ru.nl

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