Project Details
Projekt
Structural analysis of inhibitor-amyloid co-aggregates (B07)
Subject Area
Structural Biology
Term
from 2012 to 2024
Project identifier
Deutsche Forschungsgemeinschaft (DFG) - Project number 201302640
The aim of the project is to obtain an understanding of the atomic mechanisms and interactions which determine whether an amyloidogenic peptide forms a fibril or aggregates into an amorphous or oligomeric structure. In particular, we will study the conformation of Aβ aggregates in presence of αB-crystallin, and characterise the confor¬mational changes in comparison to Aβ fibril structure. In addition, we investigate cross-amyloid interaction surface mimic (ISM) inhibitors that efficiently prevent fibril formation and rescue cells from the cytotoxicity induced by Aβ. Furthermore, we will study the influence of other cellular components on the structure and the dynamics of the aggregates, which are commonly found co aggregated in vivo, such as glycosaminoglycans (GAGs) and serum amyloid P (SAP). The final goal is to understand how structural changes correlate with cellular toxicity.
DFG Programme
Collaborative Research Centres
Applicant Institution
Technische Universität München (TUM)
Project Head
Professor Dr. Bernd Reif
