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How drugs work, how they target proteins, and how humans can intervene to modulate the underlying biological processes, has always intrigued me. This is why I enrolled to study pharmaceutical science at ETH Zürich (Switzerland), one of the premier research institutions in the world. I found that I was fascinated with the early phase of drug discovery and development, particularly using structure-based drug design. I therefore joined Dr. Emil Pai’s lab at the University Health Network in Toronto (Canada) for an internship, where I was working on fluoroacetate dehalogenases and learned how to use X-ray crystallography.
For my Ph.D., I decided to join the group of Prof. Roland Riek in the Department of Chemistry and Applied Biosciences at ETH to become an expert in NMR spectroscopy. There, I successfully solved the Aβ42 fibril structure, which is the main component in plaques found in Alzheimer’s patients.
After obtaining my Ph.D., I felt the desire to find new ways of how to interfere with protein aggregation, which if successful is an important route to slow the progression of Alzheimer’s and similar diseases. Thus, I became intrigued with using chaperones to control amyloidogenic diseases, just as nature does. I joined Dr. Marius Clore’s lab at NIH (Bethesda, MD, USA) to expand my knowledge of basic NMR methodologies with one of the world’s experts and to focus on those methodologies geared towards the study of sparsely populated intermediate states which play an outsized role in the aggregation processes.Show Less
Research Opportunities
- Postdoctoral Research Assistant
Grant: Towards the Understanding of How Chaperones Function and Prevent Amyloidogenic Diseases
Courses
- BSBiological Structure 2
- PEProteins and Enzymes
Grants
- Towards the Understanding of How Chaperones Function and Prevent Amyloidogenic Diseases
Principal Investigator (PI)
2023
$249.0KActiveOpportunity
Publications (28)
Recent
- Defluorination Capability of l‐2‐Haloacid Dehalogenases in the HAD‐Like Hydrolase Superfamily Correlates with Active Site Compactness
2022
- An Efficient Method of Expression and Purification of Amyloid-Beta Aβ1–42) Peptide from E. coli
2022
- Elucidation of a nutlin-derivative—HDM2 complex structure at the interaction site by NMR molecular replacement: A straightforward derivation
2022
- Probing the Interaction of Huntingtin Exon‐1 Polypeptides with the Chaperonin Nanomachine GroEL
2021
- A weakened interface in the P182L variant of HSP27 associated with severe Charcot‐Marie‐Tooth neuropathy causes aberrant binding to interacting proteins
2021
- Visualization of sparsely-populated lower-order oligomeric states of human mitochondrial Hsp60 by cryo-electron microscopy
2021
- The three-dimensional structure of human β-endorphin amyloid fibrils
2020
- Dysregulated interactions triggered by a neuropathy-causing mutation in the IPV motif of HSP27
2019
- Rational Structure‐Based Design of Fluorescent Probes for Amyloid Folds
2019
- The NMR2 Method to Determine Rapidly the Structure of the Binding Pocket of a Protein–Ligand Complex with High Accuracy
2018
- Disassembly/reassembly strategy for the production of highly pure GroEL, a tetradecameric supramolecular machine, suitable for quantitative NMR, EPR and mutational studies
2018
- Probing the mechanism of inhibition of amyloid-β 1–42)–induced neurotoxicity by the chaperonin GroEL
2018
- Extensive sampling of the cavity of the GroEL nanomachine by protein substrates probed by paramagnetic relaxation enhancement
2018
- Chaperonin GroEL accelerates protofibril formation and decorates fibrils of the Het-s prion protein
2017
- Assignment and atomic-resolution structure of an A beta 1-42) amyloid fibril
2017
- Quenched hydrogen-deuterium exchange NMR of a disease-relevant Aβ 1-42) amyloid polymorph
2017
- Binding of polythiophenes to amyloids: Structural mapping of the pharmacophore
2017
- Fast NMR‐Based Determination of the 3D Structure of the Binding Site of Protein–Ligand Complexes with Weak Affinity Binders
2017
- Solid-state NMR sequential assignment of an Amyloid-β 1–42) fibril polymorph
2016
- NMR-based determination of the 3D structure of the ligand–protein interaction site without protein resonance assignment
2016
- Long Distance Measurements uto 160 Å in the GroEL Tetradecamer Using Q‐Band DEER EPR Spectroscopy
2016
- Atomic-resolution structure of a disease-relevant Aβ 1–42) amyloid fibril
2016
- Solution NMR Studies of Recombinant Aβ 1–42) From the Presence of a Micellar Entity to Residual β‐Sheet Structure in the Soluble Species
2015
- Protein aggregation in bacteria: functional and structural properties of inclusion bodies in bacterial cells
2014
- Contribution of specific residues of the β-solenoid fold to HET-s prion function, amyloid structure and stability
2014
- Towards a true protein movie: a perspective on the potential impact of the ensemble-based structure determination using exact NOEs
2014
- Residue‐Specific Structural Studies of Inclusion Bodies
2014
- Liquid-and Solid-State NMR Studies on the Alzheimer's Peptide and Method Development for Structure-Based Drug Design on an Oncoprotein
2014
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