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No significant changes were observed for PC LUVs (Fig. 2C).

The vesicle population was strongly concentrated for PE and a smaller but evident effect was also observed for PC LUVs (Fig. 1F,G).

This strategy was used to investigate the architecture of the peptide in the membranes of PC LUVs.

In the presence of PC LUVs, penetratin adopted mainly a random coil structure (Fig. 4A) with a negative peak around 214 nm that can be attributed to a β-sheet contribution.

In the presence of PC LUVs the peptide adopted mainly a random conformation; however, shoulders became visible at 1654 cm−1 and 1630 cm−1 corresponding to a certain amount of α-helix and β-sheet structures (Fig. 4B).

The addition of penetratin to the LUVs suspensions changed the dot distribution of PE and PC LUVs.

No significant spectral shifts were recorded after penetratin binding to PG or PC LUVs (Fig. 3D,E).

The same phenomenon, i.e. an increase in the dehydrated carbonyl absorption, although less intense, was observed with PC LUVs (Fig. 3B).

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