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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.
Research Opportunities
  • Postdoctoral Research Assistant

    Grant: Towards the Understanding of How Chaperones Function and Prevent Amyloidogenic Diseases

Courses
  • BS
    Biological Structure 2

  • PE
    Proteins and Enzymes

Grants
  • Funding agency logo
    Towards the Understanding of How Chaperones Function and Prevent Amyloidogenic Diseases

    Principal Investigator (PI)

    2023

    $249.0K
    Active
    Opportunity
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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