After graduating high school and completing his obligatory military service, Slav continued his education by pursuing a bachelor degree in Food Technology at the University for Food Technologies in Plovdiv, Bulgaria. With the completion of his bachelor in 2006, Slav decided to dive even deeper into science. As a consequence, in 2008 he landed in Wageningen University to start his master study in the Molecular Life Science program. Among many other activities during his master, Slav conducted his master thesis research in the Laboratory of Physical chemistry and Colloid science in Wageningen under the supervision of Prof. Frans Leermakers. Once that task was accomplished, Slav joined Unilever R&D center – Vlaardingen to carry out his internship under the guidance of Dr. Simeon Stoyanov and Dr. Luben Arnaudov. In 2010, he joined the Nanobiophysics group in the University of Twente as a PhD student to work on a project studying the phenomenon of self-assembly of alpha-synuclein amyloid fibrils into higher order super structures.
-Contact Information -
Slav Semerdzhiev (MSc)
University of Twente
Institute for Nanotechnology MESA+
7522 NB Enschede, the Netherlands
7500AE Enschede, the Netherlands
-Own Research in NBP-
MATERIAL PROPERTIES OF SUPRA-FIBRILLAR AGGREGATES
Alpha – synuclein (aS) is an intrinsically disordered neuronal protein capable of self-assembling in vivo into amyloid fibrils, which in turn are prone to aggregate into larger structures. aS amyloid fibrils are the main constituent of intracellular inclusions like Lewy bodies and Lewy neurites, which are distinct signatures of synucleinopathic disorders such as Parkinson’s disease. aS aggregation and amyloid formation has been a field of intensive research the past decades. However, the scope of these studies rarely has gone beyond the fibril stage of the self-assembly process. Our recent research reveals that the process continues even at larger length scales giving rise to supra-fibrillar structures with diverse but well defined morphologies. The in vitro formed supra fibrillar aggregates differ in morphology from the structures observed in vivo. This difference may be the result of the different aggregation conditions or the protein composition of the aggregates in cells. Alternatively environmental factors that are thought to play a role in Parkinson’s disease such as heavy metals and pesticides may affect inter-fibril interactions. Using wide arsenal of biophysical techniques, such as Atomic force microscopy and spectroscopy, fluorescence microscopy and many others we are trying to elucidate the factors governing the self-assembly process and the material properties of the resulting mesoscopic structures.
Schematic impression of the chronological order of events taking place during the self–assembly process of αS.
Several morphological species of supra–fibrillar aggregates formed in vitro at different experimental conditions.