Coiled-coil mediated liposomal fusion: Asymmetric behaving peptide fusogens

Membrane fusion is a vital process in living organisms and is mediated by zipper-like proteins. This thesis describes the use of coiled-coil peptides, derived from these zipper-like proteins, to mediate fusion of liposomes. Designed mutations in the peptides and in the peptide-liposome connection influences the rate and the efficiency of the fusion process. The efficiency of the fusion process is found to be very dependent on peptide structures and peptide-membrane interactions. Crucial for efficient fusion are subtle membrane interactions and very helical peptide structures. This improves our understanding of the fusion mechanism and enables the rational design of new and better fusogens. The used peptides are also able to mediate fusion between liposomes and cells and are currently used to develop drug delivery systems.NWO ChemThem grantSolid state NMR/Biophysical Organic Chemistr