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Briels den Otter Ilie Giani Ahuja Metri
Ioana M. Ilie

Ioana M. Ilie


room Carré 4029
phone +31 (0)53 489 5506
fax +31 (0)53 489 2799
e-mail i.m.ilie@utwente.nl
Ioana M. Ilie Ioana M. Ilie


Ioana M. Ilie originates from Sibiu (Hermannstadt), Romania. She obtained a PhD in Computational Biophysics in 2015 at the University of Twente. An electronic copy of her dissertation entitled Chameleon behaviour of α-synuclein. Brownian Dynamics simulations of protein aggregation can be found here. Here current research focuses on the aggregation of α-synuclein using both coarse and fine grained simulations.

Before she studied Physical Engineering at the Physics Faculty of the Babes-Bolyai Univeristy in Cluj-Napoca, which she graduated with highest honors. Later she completed a Computational Physics Master at the same University. Her research focused the flow of the aqueous NaCl solutions through carbon nanotubes under the influence of a pressure gradient, by means of Molecular Dynamics simulations. In addition, she obtained a Bachelor degree at the Business Faculty in Cluj-Napoca and a Master of Business Administration at the same Faculty. Her research focused on analyzing the competitive strategies on the Romanian pharmaceutical market and further implementing the methods on the European Solar Panel market.

Current research

Ioana Ilie Parkinson's disease affects 2% of the population aged over 65, making it not only the most common movement disorder but also the second most common neurodegenerative disease (after Alzheimer's disease). Parkinson's disease is believed to be caused by the formation of protein aggregates in the brain, by a protein called α-synuclein. α-synuclein is an intrinsically disordered protein that has the ability to change its secondary structure depending on the environment. Thus, its segments are disordered when surrounded by a solvent, curl into α-helices near a membrane or stretch into β-sheets in fibirls or amyloids. This behavior is shared by a class of amyloid-forming proteins, suggesting generic behavior.

We are investigating the formation and structure of α-synuclein aggregates by means of computer simulations. To achieve this, we are developing a highly coarse grained model by representing segments of 10-15 aminoacids as soft rigid bodies of various shapes with attractive patches on their surfaces. To simulate dynamics we have implemented a Brownian Dynamics algorithm for the translational and rotational motion.

SMPA Fundamenteel Onderzoek der Materie


A coarse grained protein model with internal degrees of freedom. Application to α-synuclein aggregation
I.M. Ilie, W.K. den Otter and W.J. Briels
J. Chem. Phys. 142, 085103 (February 2016)

Chameleon behaviour of α-synuclein. Brownian Dynamics simulations of protein aggregation
I.M. Ilie (PhD dissertation - December 2015)

An elementary singularity-free Rotational Brownian Dynamics algorithm for anisotropic particles
I.M. Ilie, W.J. Briels and W.K. den Otter
J. Chem. Phys. 142, 114103 (February 2015)

Rotational Brownian Dynamics simulations of clathrin cage formation
I.M. Ilie, W.K. den Otter and W.J. Briels
J. Chem. Phys. 141, 065101 (August 2014)