Controlling the rate of coiled coil driven membrane fusion

Tingting Zheng; Jens Voskuhl; Frank Versluis; Harshal R Zope; Itsuro Tomatsu; Hana Robson Marsden; Alexander Kros

doi:10.1039/c3cc38926j

Controlling the rate of coiled coil driven membrane fusion

Chem Commun (Camb). 2013 May 7;49(35):3649-51. doi: 10.1039/c3cc38926j. Epub 2013 Mar 27.

Authors

Tingting Zheng¹, Jens Voskuhl, Frank Versluis, Harshal R Zope, Itsuro Tomatsu, Hana Robson Marsden, Alexander Kros

Affiliation

¹ Soft Matter Chemistry, Leiden Institute of Chemistry, Leiden University, P.O. Box 9502, 2300 RA Leiden, The Netherlands.

PMID: 23531995
DOI: 10.1039/c3cc38926j

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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Circular Dichroism
Lipopeptides / chemistry*
Liposomes / chemistry*
Membrane Fusion*
Oligopeptides / chemistry*
Phosphatidylethanolamines / chemistry
Polyethylene Glycols / chemistry
SNARE Proteins

Substances

1,2-dioleoyl-glycero-3-phosphatidyl ethanolamine
Lipopeptides
Liposomes
Oligopeptides
Phosphatidylethanolamines
SNARE Proteins
Polyethylene Glycols