Is efficiency of protein incorporations governed by membrane properties? An α-synuclein and ceramide-1-phosphate investigation.

In protein-membrane interactions membranes provide an environment that enables proteins to fulfill multiple functions. Yet our knowledge about specificity of protein-membrane interactions is not sufficient. It is our hipothesis that this specificity is governed to a large extend by the properties of membrane itself. This study investigates the protein-membrane interactions in the case of -synuclein (S) and ceramide-1-phosphate (C1P) enriched membranes. The interactions between S and lipids were reported to be governed by various factors, including lipid composition, membrane curvature, charge and fluidity. On the other hand, C1P is anionic lipid and the shape of its molecule is similar to that of PA, which was reported to strongly interact with S. There are three main aspect of this work. First of all interactions between S and C1P enriched membranes is investigated using microscale thermophoresis. Secondly, systematic characterization of membrane systems is performed using both in vitro and in silico techniques. Eventually, principal component analysis and multiple linear regression are used to determine phenomenological dependency of those interactions in function of membrane properties.