Nanoreactors formed from self-assembled protein cages

Reconstruction of the structures of the Cowpea Chlorotic Mottle Viru

Reconstruction of the structures of the Cowpea Chlorotic Mottle Virus determined by X-ray crystallography and cryo-electron microscopy. Full capsid structure (left) and view of the inner cavity of the virus (right). (From CM Shepherd et al., (2006). VIPERdb: a relational database for structural virology. Nucl. Acids Res. 34, D386. http://viperdb.scripps.edu/).
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Developing new biological materials

At the interface of biology, chemistry and materials science we are developing novel approaches to the formation of materials, e.g. exploiting biomolecular self-assembly and organisation for the templated construction of new materials. Viruses such as the well-characterised Cowpea Chlorotic Mottle Virus (CCMV) are intrinsically attractive scaffolds because they consist of a highly stable, symmetrical, protein shell (called capsid), which is self-assembled from small proteins and encloses the viral RNA.

By Small Angle Neutron Scattering on LOQ, we have examined the sensitivity of the CCMV capsid in D2O to pH and ionic strength of the surrounding environment. Fitting using a core-shell spherical model shows that there is almost no change in the outer diameter going from the virus to the capsid at pH 5 (27 vs. 26nm) but that it decreases upon going to higher pH (pH 6.5, 23nm; pH 7.5, 17nm) with a concomitant increase in polydispersity.

M Comellas-Aragones, FD Sikkema, JJLM Cornelissen, MC Feiters, RJM Nolte (Nijmegen University, The Netherlands), D Visser (NWO, The Netherlands), AE Terry, RK Heenan (ISIS)

Research date: December 2006

Further Information

Prof MC Feiters, [mcf@sci.kun.nl] DM Vriezema et al., Chem. Rev. 105 (2005) 1445

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