Herein, we demonstrated for the first time that hydrophobic ion pairing is a promising strategy to enhance peptide entrapment within liposomes. Indeed, pre-forming hydrophobic peptide-surfactant ion pairs prior to entrapment into the liposomes was deemed to be the most promising approach to producing peptide loaded monodispersed liposomes. The teriparatide loading ranged between 10 -30 µg of teriparatide per mg of lipid. A range of different teriparatide loading levels up to 70 µg per mg of liposome was achieved by adapting the amount of peptide ion pair dispersion (0.1 mL -0.85 mL per mL) that is added to the phospholipid mixture prior to formation of the thin film (Figure ). From Figure it can be observed that the increase in hydrophobic ion pair loading is inversely correlated with entrapment efficiency. Where the volume has been increased from 100 µL of ion-pair solution/dispersion to 850 µL a decrease in entrapment from 70% to 40% was observed. The decrease in entrapment appears to stabilise around 30-40% within the tested range. While the increase in ion-pairs incorporated within the thin-film resulted in a decrease in entrapment, an increase in peptide loading was observed from 7.5 µg/mg of liposomes up to 70 µg/mg within the range explored. The decrease in entrapment efficiency is due to the increase in drug:lipid ratio. As lipid concentrations are relatively low (<15 mM), this could be improved by increasing the lipid concentration .