Última modificación: 05/12/2019 - 09:10
Dr. Javier Oroz (Instituto de Química Física Rocasolano, CSIC, Madrid)
Structural biology in human disease: What can we learn from the study of disordered proteins?
The critical toxic species in over 40 human diseases are misfolded proteins, which undergo structural changes in response to different triggers or modulators that lead to aberrant folds prompting their toxicity and cell death. These pathogenic processes frequently lead to formation of amyloid aggregates in the senescent cells, which are characteristic of some devastating diseases such as Alzheimer’s, Parkinson’s or Amyotrophic Lateral Sclerosis, among others. Fueled by the vast socio-economic impact of these amyloid diseases, intense research over the last decades has enabled the understanding of many crucial molecular processes that determine the progress of these diseases. However, we lack a mechanistic understanding of the early misfolding changes in amyloid proteins that trigger toxicity, aggregation and the development of the disease. In this talk, I will review the current knowledge on the structural basis of pathogenic amyloidosis and why this is highly relevant for the development of active biomarkers or therapeutics for the diseases. Because most of amyloid proteins are intrinsically disordered, Nuclear Magnetic Resonance (NMR) spectroscopy is the only high-resolution structural technique that enables the study of their structural properties in disease. I will focus on the discoveries on amyloidogenic proteins that we have achieved by NMR and present a perspective of what are the main bottlenecks currently faced and the lines of research that will be launched in the near future.
DIA Y HORA: 13 DICIEMBRE A LAS 12:30
LUGAR: SALA DE CONFERENCIAS, EDIFICIO I+D+i,
CAMPUS RIO EBRO