Surface behavior of α-Synuclein and its interaction with phospholipids using the Langmuir monolayer technique: a comparison between monomeric and fibrillar α-Synuclein.
Academic Article
Overview
abstract
Due to the involvement of α-Synuclein (α-Syn) in lipid transport and its role in the normal function and in the pathology of Parkinson disease, it is important to study first the surface properties of the protein at the air/water interface and second its behavior related to biological membranes. For this purpose, the monomolecular film technique was used as membrane model to compare the interactions with various phospholipids of monomeric and fibrillar forms of α-Syn. We have determined the equilibrium surface pressure of the two forms of α-Syn (monomeric and fibrillar form) at the air/water interface. The surface pressures reached by monomeric α-Syn were shown to be higher than the ones of fibrillar α-Syn and similar to the value obtained by mellitin, a lytic peptide of bee venom, which has been described as "protein detergent". The monomeric α-Syn adsorbed more rapidly at the air/water interface with a maximal adsorption rate at least 60-times higher than the fibrillar form. In the presence of a phospholipid monolayer, the surface activities of two α-Syn forms are much greater than observed at the air/water interface. Also we can show that the fibrillar form of α-Syn have a higher value of critical pressure than the monomeric one for the cow brain extract and the Phospatidyl Glycerol (an anionic phospholipid) which confirm its higher affinity for the anionic phospholipid than the monomeric form. According these results, we can suggest that this aggregate form have important implications for the pathological activity and, therefore, for the associated neurotoxicity which can results in layer disruption and cell leakage.
