A virus-based single-enzyme nanoreactor

M. Comellas-Aragones, H. Engelkamp, V.I. Claessen, N.A.J.M. Sommerdijk, A.E. Rowan, P.C.M. Christianen, J.C. Maan, B.J.M. Verduin, J.J.L.M. Cornelissen, R.J.M. Nolte

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348 Citations (Scopus)


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.
Original languageEnglish
Pages (from-to)635-639
JournalNature Nanotechnology
Issue number10
Publication statusPublished - 2007


  • fluorescence correlation spectroscopy
  • tobacco-mosaic-virus
  • protein
  • molecule
  • cage
  • encapsulation
  • organization


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