Biophysics of neurodegenerative diseases
10:00 EST / 15:00 GMT / 16:00 CET
Astbury Professor of Biophysics and Royal Society Research Professor, University of Leeds
Professor of Molecular Cell Biology, Johannes Gutenberg University Mainz, Adjunct Director at the Institute of Molecular Biology (IMB) in Mainz
Professor of Biology and Chemistry, Head, Department of Biological Sciences; Indian Institute of Science Education and Research (IISER) Mohali, Visiting Professor, Indian Institute of Technology (IIT) Bombay, Mumbai
Director of Publications, Biophysical Society
Proteins are the molecular workhorses of life. In order for them to perform their physiological function, they need to be folded into unique 3D structures. The misfolding and aggregation of proteins into amyloid fibrils are associated with debilitating neurodegenerative diseases such as Alzheimer’s, Parkinson’s, Huntington’s, prion diseases, amyotrophic lateral sclerosis (ALS), and so forth. Additionally, a class of proteins that does not autonomously fold up into unique 3D structures, called intrinsically disordered proteins, can also attain the amyloid state via the protein misfolding pathway or via the aberrant phase separation-mediated pathway. It is therefore important to understand the fundamental biophysical mechanism behind these protein misfolding diseases as well as to design small molecules that can be used as potent inhibitors of the aggregation process.
In this webinar hosted by the Biophysical Journal, Sheena Radford (University of Leeds, UK), Dorothee Dormann (Johannes Gutenberg University and Institute of Molecular Biology, Mainz, Germany), and Samrat Mukhopadhyay (Indian Institute of Science Education and Research, Mohali, India) will address some of the challenges in the field and new biophysical insights into the formation and inhibition of pathological protein aggregates.