BECAS MAX PLANCK / FUNDACIÓN BUNGE Y BORN / FUNDACIÓN WILLIAMS

Concurso

2013

Amyloid proteins in neurodegeneration: From structural and cellular biology to therapy

Ariel Alejandro Valiente Gabioud

Max Planck Institute for Biophysical Chemistry

The misfolding of proteins into a toxic conformation is proposed to be at the molecular foundation of a number of neurodegenerative disorders including Alzheimer and Parkinson’s disease. One common and defining feature of protein misfolding diseases is the formation and deposition of amyloid-like fibrils. Currently, no preventive therapy is available for Parkinson and Alzheimer diseases. Identification of therapeutic drugs is not only complicated by a lack of understanding of many of the key aspects of the pathogenesis of these diseases but also by the multifactorial etiology of them. The aggregation pathway of the proteins linked to these disorders represents then an obvious target for therapeutic intervention. The detailed understanding of the phenomenon of amyloid fibrillation and its inhibition is therefore highly clinically important. The general purpose of this project research is to study the structural and toxic mechanisms related to amyloid formation and understand the structural and molecular basis behind the aggregation inhibitory effects of small molecules in order to advance in the rational design of a therapeutic strategy based on amyloid inhibitors. These goals will be achieved using a combination of biophysical and biochemical approaches as well as in vivo experiments.

RECIBÍ NUESTRAS NOVEDADES

SEGUINOS

  • LinkedIn - Gris Círculo
  • Facebook - Gris Círculo
  • YouTube - Gris Círculo
  • Instagram - Gris Círculo
  • RSS - Gris Círculo

Somos una organización sin fines de lucro fundada en 1963, con sede en Buenos Aires, Argentina. Promovemos el conocimiento y la innovación en beneficio de nuestra sociedad.

Tel. +54 (11) 4318-6600

25 de Mayo 501 6º Piso

Ciudad Autónoma de Buenos Aires

ARGENTINA

©2019 Fundación Bunge y Born / Política de privacidad