Dialysis was investigated as an alternative for purification of liposomes from unentrapped peptide. The initial optimisation was done using 100 kDa Float-A-Lysers (1mL) offering the potential from scale-up of up to 10 mL as well as processing several batches simultaneously. Empty liposomes were spiked with teriparatide to a final concentration of 1 mg/mL of peptide. The peptide spiked liposomal formulation was filled into 100 kDa Float-A-Lysers and dialysed against 600 mL of 100mM phosphate buffer (pH = 7.4). After pre-defined timepoints, a small sample of liposomal formulation was withdrawn from within the dialysis tube, and peptide content was measured. Figure .1 shows the percentage of free teriparatide that was removed from the liposomal formulation by dialysis over a 24h period. It can be observed that the liposomal formulation was free of unencapsulated peptide after 4h (98% removed) with >99% removed after 24h. Dialysis was deemed suitable for purification of liposomal formulations with samples typically dialysed overnight (~16h).