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Homo & hetero-oligomeric foldomes of functional and pathological amyloids

  Challenge: Neurodegeneration

PI: Miguel Mompeán

     

Critical aspects relating protein aggregation to cell function and human disease are still unknown. We wish to understand what structural, thermodynamic and kinetic factors drive the preferential assembly of some aggregate forms over others (e.g. homo- versus hetero-amyloids versus intrinsically disordered forms within condensates). Using and re-thinking advanced NMR methods in solution and in the solid-state, including hyperpolarization schemes and a myriad of computational approaches, we aim to identify the defining features of functional versus pathological aggregate forms in relevant health-related proteins, including TDP-43, nucleoporins and RIP kinases and other RHIM-containing proteins. This knowledge is ultimately used to design new proteins that modulate distinct aggregation events

Web Figure research1

In the figure, a droplet (top left) and a fibril form (bottom left) of a protein, and the structural model of a hetero-amyloid (right).

 

Publications

Collaborators

  • Ann McDermott (Columbia University, New York, United States)
  • Emanuele Buratti (International Centre for Genetic Engineering and Biotechnology, ICGEB, Trieste, Italy)

Financing

  • La Caixa Banking Foundation – Junior Leader Programme