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CPP: Fachverband Chemische Physik und Polymerphysik
CPP 13: Membranes and Vesicles (joint session BP/CPP)
CPP 13.4: Vortrag
Montag, 16. März 2020, 10:15–10:30, ZEU 250
Structural and dynamical changes of biomimetic myelin membranes induced by myelin basic protein — •Benjamin Krugmann1, Andreas Stadler2, Aurel Radulescu1, Alexandros Koutsioumpas1, Marie-Sousai Appavou1, Martin Dulle2, Laura Stingaciu3, and Stephan Förster2 — 1FZJ JCNS-1, 52428 Jülich, Germany — 2FZJ JCNS-MLZ, 85748 Garching, Germany — 3ORNL, Oak Ridge TN 37831, USA
A major component of the saltatory nerve signal conduction is the multilamellar myelin membrane around axons. In demyelinating diseases like multiple sclerosis, this membrane is damaged. In literature different values for the lipid composition of healthy myelin sheath and myelin with experimental autoimmune encephalomyelitis - the standard animal model for multiple sclerosis - have been found. In this work we try to elucidate the interaction mechanism of myelin basic protein - the structural protein responsible for the cohesion of the cytoplasmic leaflets of the myelin sheath - with membranes mimicking both compositions. As samples we use unilamellar vesicles and supported bilayer systems. With neutron and x-ray small angle scattering methods combined with cryo-TEM we can follow the rapid aggregation which leads to a slow process in which different structures are formed depending on the lipid composition. Those structural information can be associated with the bending rigidity of the respective membrane measured with Neutron Spin Echo. Neutron reflectometry gives insights on how the interaction mechanism between membrane and protein functions and reveals how modified membranes are destabilised by the protein.