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.
Original language | English (US) |
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Pages (from-to) | 1848-1851 |
Number of pages | 4 |
Journal | Biophysical journal |
Volume | 108 |
Issue number | 8 |
DOIs | |
State | Published - Apr 21 2015 |
Bibliographical note
Publisher Copyright:© 2015 Biophysical Society.