Icosahedral protein capsids are useful for the storage, transport, or regulation of encapsulated cargo molecules. These structures are attractive for various applications in bionanotechnology, though a better understanding of their supramolecular chemistry is needed. Lumazine synthase from Aquifex aeolicus (AaLS) self-assembles into a 60-subunit dodecahedral capsid and provides an appealing scaffold for engineering novel encapsulation systems. However, an inability to control AaLS capsid assembly has presented a major obstacle for cargo loading in vitro. Through deconstruction of this capsid into its constituent pentamers by rational design we were able to identify structural determinants for AaLS capsid assembly. This understanding allowed us to generate a redox switch for triggering capsid assembly in vitro via covalent modification of the pentamers. It is anticipated that this engineered capsid assembly switch will enable the encapsulation of cargo molecules in vitro, which should prove useful in the construction of novel drug delivery and catalytic systems.

Deconstructing and reconstructing a protein capsid

245th National Meeting (2013)

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