Team Members

Funtional and pathological protein aggregation, membrane protein folding, protein-detergent interactions

My research interests are mainly focused on the topics of protein fibrillation, nanoparticles-proteins interactions, and protein and peptide self-assembly. In my research activity I have used different techniques, such as ThT assays, Circular Dichroism (CD), fluorescence based techniques, Small-angle X-ray scattering (SAXS), and isothermal titration calorimetry (ITC).

Protein aggregation and oxidation

Membrane protein folding

Glycosaminoglycans in protein aggregation.

Protein aggregation using NMR

Exploring the potential of liprotides: Protein-lipid complexes

Peptide stability and formulation.  

Vitamin D fortification using protein-lipid complexes

Alpha-synuclein and bacterial amyloid proteins.

I am currently working on generating and characterizing toxic protein oligomers involved in different neurodegenerative diseases. Main focus: tau and Alzheimer’s disease.

Potential stabilizing effect of nanobodies on fibrillation prone proteins

working with transformation and purification of GLPG and analysis on membrane proteins

Alpha-synuclein oligomers (aSOs) are believed to play a major role in PD pathology. aSOs come in different sizes and shapes and also different toxic mechanisms have been described. In order to gain more insight in PD pathology, the main goal of my project is to identify an aSO binding partner.

Working with GalR aggregation, refolding studies, peptide array self-recognition of functional amyloids and GlpG rhomboid membrane protease.