Liposome Deformation Induced by Membrane-Binding Peptides

This paper presents an investigation of liposome deformation and shape distortion using four membrane-binding peptides: TAT and C105Y as cell-penetrating peptides (CPPs), and melittin and ovispirin as antimicrobial peptides (AMPs). Liposome deformation was monitored utilizing fluorescent microscopy, while the binding of peptides to the DOPC membrane was estimated through capacitance measurements. The degree of liposome deformation and shape distortion was found to be higher for the CPPs compared to the AMPs. Additionally, it was observed that C105Y did not induce liposome rupture, unlike the other three peptides. We propose that these variations in liposome distortion may be attributed to differences in secondary structure, specifically the presence of an alpha-helix or random coil. Our studies offer insight into the use of peptides to elicit control of liposome architecture and may offer a promising approach for regulating the bodies of liposomal molecular robots.

Automated summary

This study investigates the deformation and shape distortion of liposomes using four membrane-binding peptides: TAT and C105Y as cell-penetrating peptides (CPPs), and melittin and ovispirin as antimicrobial peptides (AMPs). Liposome deformation was observed using fluorescent microscopy, while peptide binding to the DOPC membrane was estimated through capacitance measurements. It was found that the CPPs caused higher liposome deformation and shape distortion compared to the AMPs, and C105Y did not induce liposome rupture unlike the other three peptides. The differences in liposome distortion may be attributed to variations in secondary structure. These findings provide insights into controlling liposome architecture using peptides and have implications for regulating liposomal molecular robots.