Finally, we attempted to study the cooperative ion transport by SSA 1 and anionophore 4 using conductance measurements We hoped to gain insight into the potential transport mechanism of SSA 1; based on the small molecular size of this SSA, it cannot feasibly form a unimolecular, membrane-spanning structure; however, given the reported self-assembly capabilities of SSAs, 15a, 15b we considered the formation of self-assembled channels a distinct possibility. We performed conductance measurements across DPhPC with 10 % cholesterol planar phospholipid bilayers using a Port-a-Patch miniaturised patch clamp system (see Section S4). This lipid cholesterol mixture was selected as it allowed for the formation of a stable lipid bilayer under these experiment conditions. We found that at lower concentrations (≤ 0.25 mM), the addition of SSAs 1-3 and 4 alone did not produce an elevated current recording over the experimental timeframe (Figure (a)). At higher concentrations of SSA, we observed bilayer rupture (Figure 4(b)). Here, the SSA acts as a simple surfactant, effectively destroying the phospholipid planar bilayer. However, under specific conditions, the addition of SSA 1 and anionophore 4 together produced an erratic, elevated current flow across the clamped portion of the bilayer, until eventual bilayer rupture was observed ≈ 210 seconds after SSA addition (Figure 4(c)). Notably, we observed changes in membrane potential on the nA rather than pA scale ≈ 30 seconds after SSA addition. We believe this 'lag phase' in observable activity is due to the time taken for the SSA to arrive and partition into the planar bilayer before any effects can be observed. These data suggest that a critical concentration of SSA is required at the bilayer surface to initiate ion transport events. However, when these events are initiated, they result in enormous changes in membrane potential, before full bilayer rupture. We therefore suggest that SSA 1 operates in combination with anionophore 4 to initiate concentration dependent bulk ion transport events. We also performed conductance measurements with an increased number of data points collected with respect to time (Figure ). The observed data are not consistent with the controlled, stepwise, open/ close behavior of single ion channels that is commonly reported for biological and synthetic ion channels, particularly given the magnitude of the current fluctuations. However, we suggest that these concentration dependent mass ion transport events (over a time period ≤ 0.7 seconds) could be representative of SSA 1 operating though a mechanism analogous to that of the antimicrobial peptide "carpet model" in the presence of anionophore 4. In this model, peptides accumulate on the bilayer surface until they reach a critical concentration at which membrane disruption can occur. 23b