The utility of hydroxy double salts (HDSs) for the uptake and delivery of a range of functional anions via ion exchange is demonstrated. Three novel HDS nanocomposites containing medicinal (ibuprofen and diclofenac) and agrochemical (2,4,5-trichlorophenoxyacetic acid) species have been synthesised through ion exchange intercalation. The release of the guest ions from the host has subsequently been explored. A range of models have been applied to the release kinetics. Release of 2,4,5trichlorophenoxyacetic acid took place over ca. 200 minutes and release of ibuprofen over around 250 minutes. Coating the crystallites of the intercalates with a sodium alginate layer led to release times being extended to approximately 10 hours, which is an appropriate timescale for an effective release system.

In a number of membrane-bound viruses, ion channels are formed by integral membrane proteins. These channel proteins include M2 from influenza A, NB from influenza B, and, possibly, Vpu from HIV-1. M2 is important in facilitating uncoating of the influenza A viral genome and is the target of amantadine, an anti-influenza drug. The biological roles of NB and Vpu are less certain. In all cases, the protein contains a single transmembrane ␣-helix close to its N-terminus. Channels can be formed by homo-oligomerization of these proteins, yielding bundles of transmembrane helices that span the membrane and surround a central ion-permeable pore. Molecular modeling may be used to integrate and interpret available experimental data concerning the structure of such transmembrane pores. This has proved successful for the M2 channel domain, where two independently derived models are in agreement with one another, and with solid-state nuclear magnetic resonance (NMR) data. Simulations based on channel models may yield insights into possible ion conduction and selectivity mechanisms.