Evolutionary conservation of metamorphic switches.

About us.

Our research group is dedicated to understanding how protein polymorphism and structural plasticity shape biological function and dysfunction. Proteins are not static entities; many can adopt multiple conformations depending on their environment, interaction partners, or cellular conditions. This structural versatility is essential for normal cellular processes but it can also drive pathology. PLASTIMORF leverages cutting-edge structural, orthogonal and translational techniques to unravel mechanisms behind protein structural changes that lead to a prion-like gain-of-function.

We investigate how distinct structural states of the same protein emerge, coexist, and interconvert, and how this polymorphism influences biological outcomes. A central focus of our work is determining how structural variability contributes to the onset and progression of neurodegenerative diseases. Yet, we also explore protein aggregation as molecular patformsm that provide new functional responses.

By combining biophysical, structural, and biochemical approaches, we characterize proteins across different states ranging from soluble and intrinsically disordered forms to phase-separated condensates and solid aggregates.

We aim to uncover:
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- The molecular determinants that govern structural transitions as fundamental understanding to generate pioneering biomedical tools
- Coupling of phase separation and amyloid aggregation
- Molecular modulators of polymorphic aggregation

- Homorepeats in neuronal proteins: Implications in function and human disease

- Plant prionoids as adaptation platforms towards global warming

Our ultimate goal is to bridge molecular structure with biological consequence: to understand not only how proteins change shape, but what those changes mean in their physiological and pathological contexts. Through this integrative approach, we seek to provide fundamental insights that may inform future therapeutic strategies targeting protein misfolding and aggregation or enhancing protein modifications for better functionality.