Atomic-scale biology of prions and other amyloids: structure, mechanism, disease
Main focus: prions as a paradigm of neurodegeneration

Prions are fatal pathogens that attack the brains of humans and animals. Unlike most infectious agents, prions are composed solely of protein. They arise from misfolded chains of the membrane-bound glycoprotein prion protein (PrP), which assemble into infectious amyloid fibrils. Remarkably, different prion strains vary in transmissibility, and cross-species barriers often limit infection.

Despite decades of research, we still do not fully understand how prions and other amyloids replicate in living systems, or how their accumulation in the brain and other tissues drives neurodegeneration and other diseases.

My laboratory seeks to uncover the molecular mechanisms underlying the propagation and toxicity of prions and other amyloids. To do this, we employ state-of-the-art biomedical research approaches, including genetic code expansion (GCE) and bioorthogonal fluorescent labeling, click chemistry, single-molecule localisation microscopy (SMLM), in situ (in-cell) correlative light and electron cryo-microscopy (cryo-CLEM), cryo-electron tomography (cryo-ET), single-particle cryo-EM, soft X-ray tomography (cryo-SXT), and more.