anja_stefanovic

-Short Biography

During my high school education I was especially interested in chemistry, physics and informatics, but on the day of qualification exams for University I decided to study something more medically and biochemistry related. On that warm day in 2003 I made my choice choosing Faculty of Pharmacy at University of Belgrade as my future career. At the beginning I decided to take a course in medical biochemistry because I always enjoyed working in the lab so I thought that will be a perfect solution. During my study I obtained knowledge in biology, physics, physical chemistry, mathematics and also 14 different types of chemistry. Also I was active as study group representative in Student Parliament of Faculty of Pharmacy from 2004 till 2006. All the time of my studies I had a state scholarship. After 4th year I did my traineeship in a hospital for three weeks. In January 2009 I defended my Master thesis Inborn metabolic disease as the first one in generation in my course and became MSc of pharmacy-medical biochemist. Immediately afterwards I started my internship in Clinical-biochemistry laboratory in Institute for Medical Biochemistry and Institute for Cardiovascular Disease, Clinical Center of Serbia, Belgrade. During my internship I was also involved in a science project Influence of antioxidative parameters (enzymes, FVII, FVIII, vWF) in cardiovascular diseases. Because of my interest in science in October 2009 I started my research project Single cell analysis in microfluidics based chip devices in BIOS group, University of Twente. After that in April 2010 I joined Nanobiophysics group as a PhD student and I am currently working on a project Oligomer-phospholipid bilayer interactions - the mechanism of membrane disruption.

In my free time I am enjoying travelling, sightseeing, long walking and fitness.

-Contact Information -

Anja Stefanović (MSc)

Nanobiophysics

University of Twente

Institute for Nanotechnology MESA+

Zuidhorst ZH167

Drienerlolaan 5

7522 NB  Enschede, the Netherlands

PO-box 217

7500AE Enschede, the Netherlands

P +31-(0)53-489-4612

M +31-(0)61-633-5365


a.stefanovic@utwente.nl

-Own Research in NBP

Oligomer-phospholipid bilayer interactions - the mechanism of membrane disruption.

The interaction of oligomeric α-synuclein with membrane systems has been involved in both normal functions of the protein and in the pathophysiology of Parkinson's disease. The key question is how oligomers interact with membrane systems and what the influence of their interaction is. It is known that oligomeric α-synuclein can permeabilize cellular membrane by interfering with calcium pathways. Also, membrane permeabilization by oligomeric αS is maybe associated with the pathological mechanism of neuronal cell death in PD. To mimic cellular membrane compositions we are investigating binding and permeabilization of oligomeric and monomeric αS to vesicle systems composed of physiologically relevant lipid mixtures. Comparing leakage and binding of physiologically relevant lipid compositions can rip up biophysical properties of cellular membrane. For permeabilization of α-synuclein presence of negatively charged lipids is necessary event but whether aS can bind and permeabilize membranes with physiologically relevant lipid compositions has not been extensively explored. Therefore, we want to determine the mechanism of membrane-α –synuclein interactions in vivo and in vitro as well which can shed us a light on possible mechanism of Parkinson's disease. This will allow us to study the role of αS oligomers in the pathogenesis of Parkinson`s disease.

Publications of interest

1.

B.D. van Rooijen, M.M.A.E. Claessens, V. Subramaniam. Membrane binding of oligomeric a-synuclein depends on bilayer charge and packing, FEBS Letters 582 (2008) 3788–3792

2.

G. van Meer, D.R. Voelker, G.W. Feigenson, Membrane lipids: where they are and how they behave, Nature Reviews Molecular Cell Biology 9 (2008), 112-124

3.

D.S. Dimitrov, M.I. Angelova, Swelling and electroswelling of lipids: theory and experiment, Studia Biophysica 113 (1986), 1-2: 15-20