Mr. Jendrik Marbach

Mini Academic CV

University degrees:

First degree or intermediate examination:

  • Bachelor of Science

Second degree and/or intermediate examination:

  • Master of Science

Attended conferences:

  • "Stem Cell Network North Rhine Westphalia" , Herne
  • "Stem Cell Network North Rhine Westphalia", Aachen

Prices/Scholarships:

  • Dr. Jost Henkel Stipendium 2009

BioStruct PhD project

Structural analysis of membrane-anchored prion proteins and protein protein interaction within the membrane
Prion diseases like Creutzfeldt Jakob disease are an unique group of transmissible neurodegenerative diseases which can also occur spontaneously or have a genetic background. The infectious particles are termed prions. The main component of prions is a misfolded conformer (PrPSc) of a normal glycosylated cell surface protein, the cellular prion protein (PrPC), whose function is unknown in detail (for review see: Prusiner 2007, Fields Virol. 3059-91). During replication of prions, PrPC is converted into PrPSc. We investigated the conversion process by in vitro studies with several biophysical methods using recombinant PrP and natural PrPSc. We identified intermediates and precursor states during the conversion process and investigated the kinetics of spontaneous as well as seeded fibrillogenesis (for review see: Birkmann et al., 2008, Prion, 2 (2), 67-72). The non-infectious PrPC undergoes several posttranslational modifications, in particular attachment of two N-linked glycans and a glycosylphosphatidylinositol (GPI)-anchor, by which it is linked to the plasma membrane on the exterior cell surface. We studied the interaction of posttranslationally modified PrPC from Chinese hamster ovary cell culture (CHO-PrP) with model membranes in vitro, i.e. either with lipid vesicles in solution or lipid bilayers bound on a chip surface (Elfrink et al., Biol. Chem. 2007: 388(1):79-89). The equilibrium and mechanism of PrPC-association with model membranes was analyzed by surface plasmon resonance (SPR) and the ratio between free and membrane-attached CHO-PrPC was quantified. It is not known in which part of the cell PrPC and PrPSc interact and where the conversion takes place. One hypothesis is that the interaction takes place at the cell membrane. Within this project we aim at the structural and biophysical analysis of PrPC in the membrane.

Supervisors

Topic Supervisor:

undefinedDr. Eva Birkmann, ISB-3 / Structural Biochemistry, Forschungszentrum Jülich, Birkmann Group

Complementary Supervisor:

undefinedProf. Dr. Henrike Heise, Institute of Physical Biology, Heinrich Heine University Duesseldorf, Heise Group

Responsible for the content: E-MailBioStruct Office