title: Controlling the rate of coiled coil driven membrane fusion.
abstract: Sets of complementary lipidated coiled-coil forming peptides that fuse membrane fusion have been designed. The influence of the coiled-coil motif on the rate of liposome fusion was studied, by varying the number of heptad repeats. We found that an increased coiled-coil stability of complementary peptides translates into increased rates of membrane fusion of liposomes.
authors.affiliation: Soft Matter Chemistry, Leiden Institute of Chemistry, Leiden University, P.O. Box 9502, 2300 RA Leiden, The Netherlands.
authors.forename: Tingting
authors.initials: T
authors.lastname: Zheng
authors.forename: Jens
authors.initials: J
authors.lastname: Voskuhl
authors.forename: Frank
authors.initials: F
authors.lastname: Versluis
authors.forename: Harshal R
authors.initials: HR
authors.lastname: Zope
authors.forename: Itsuro
authors.initials: I
authors.lastname: Tomatsu
authors.forename: Hana Robson
authors.initials: HR
authors.lastname: Marsden
authors.forename: Alexander
authors.initials: A
authors.lastname: Kros
mesh_terms: D002942:Circular Dichroism; D055666:Lipopeptides / Q000737:chemistry*; D008081:Liposomes / Q000737:chemistry*; D008561:Membrane Fusion; D009842:Oligopeptides / Q000737:chemistry*; D010714:Phosphatidylethanolamines / Q000737:chemistry; D011092:Polyethylene Glycols / Q000737:chemistry; D050600:SNARE Proteins
chemical_list: C410262:1,2-dioleoyl-glycero-3-phosphatidyl ethanolamine; D055666:Lipopeptides; D008081:Liposomes; D009842:Oligopeptides; D010714:Phosphatidylethanolamines; D050600:SNARE Proteins; D011092:Polyethylene Glycols