title: α-Synuclein Reduces Tension and Increases Undulations in Simulations of Small Unilamellar Vesicles.
abstract: Using coarse-grained molecular dynamics simulations we have explored the effect of α-Synuclein (αSyn) on the structural and mechanical properties of small unilamellar vesicles in the fluid-phase. The study is motivated by observations that a high density of membrane-bound αSyn inhibits the fusion of synthetic small unilamellar vesicles. By combining three-dimensional pressure tensor calculations with our recently developed spherical harmonics fluctuation analysis approach, we show a reduction in membrane surface tension and increased membrane undulations when αSyn is bound to the vesicle's outer leaflet at a 200:1 L/P. The protein effects these changes by decreasing the negative pressure in the headgroup region of the outer leaflet and increasing the positive pressure throughout the hydrocarbon core.
authors.affiliation: Department of Biomedical Engineering, University of Minnesota, Minneapolis, Minnesota.
authors.forename: Anthony R
authors.initials: AR
authors.lastname: Braun
authors.affiliation: Department of Biomedical Engineering, University of Minnesota, Minneapolis, Minnesota. Electronic address: jnsachs@umn.edu.
authors.forename: Jonathan N
authors.initials: JN
authors.lastname: Sachs
mesh_terms: D015060:1,2-Dipalmitoylphosphatidylcholine / Q000737:chemistry; D011485:Protein Binding; D013314:Stress, Mechanical; D053835:Unilamellar Liposomes / Q000737:chemistry*; D051844:alpha-Synuclein / Q000737:chemistry* / Q000378:metabolism
chemical_list: D053835:Unilamellar Liposomes; D051844:alpha-Synuclein; D015060:1,2-Dipalmitoylphosphatidylcholine