Physical Chemistry

Lund University

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Amyloid interaction with lipid membranes

Amyloid protein aggregation is associated with over 30 known diseases in humans. In amyloid plaques associated with several amyloidogenic diseases, tightly associated lipids have been identified. For several of the amyloid disorders, protein aggregation has also been associated with membrane disruption in cells and in model lipid systems. In this project, we investigate interactions between aggregating amyloid proteins and lipid membranes, and we explore the basic principles of the amyloid-lipid coaggregation.

The proteins α-synuclein  is found in the protein aggregates characteristic for Parkinson disease. In this project, we study interactions between  α-synuclein and lipid membranes. We use model membranes with varying lipid compositions, and biological membranes in isolated exosomes. We study protein-lipid co-aggregation, membrane assoication and the consequences of protein-lipid interaction on aggregation kinetics and membrane intergrety. In this project we explore different biophysical techniques, including PT ssNMR, confocal microscopy on giant unilamellar vesicles, fluorescence correlation spectroscopy, fluorescence spectroscopy, QCM-D, neutron reflectivity and cryo-TEM.

People:  Ricardo Gaspar, Ilaria Idini, Aleksandra Dabkowska, Veronica Lattanzi, Sara Linse (Division of Biochemistry and Structural Biology, LU), Tommy Nylander, Ulf Olsson, Daniel Topgaard, Celine Galvagnion (Cambridge University, UK).

Contact person: Emma Sparr