Protein Misfolding and Amyloid Diseases

TUM-IAS Hans Fischer Senior Fellow Prof. Ayyalusamy Ramamoorthy (University of Michigan) worked in this Focus Group with his host Prof. Bernd Reif (Solid-State NMR, TUM).

Our research group was primarily focused on solving the high-resolution structures of oligomeric intermediates of amyloid proteins (such as amyloid-beta and amylin (or IAPP)) and investigating their membrane interactions that are linked to cell toxicity by using a combination of solution and solid-state NMR and other biophysical techniques. Some of the specific topics include:

  1. Misfolding, aggregation, and cell toxicity of human islet amyloid polypeptide (IAPP).
  2. Mechanisms of membrane disruption by amyloid-beta (related to Alzheimer's Disease) and IAPP (implicated in type-2 diabetes).
  3. Atomic-level resolution structures and dynamics of amyloid protein intermediates by NMR.
  4. Effects of amyloid inhibitors on the structure and toxicity of abeta and IAPP.

Diana Rodriguez (2015-2017, TUM)

Publications by the Focus Group


  • Rodriguez Camargo, Diana C.; Tripsianes, Konstantinos; Buday, Katalin; Franko, Andras; Göbl, Christoph; Hartlmüller, Christoph; Sarkar, Riddhiman; Aichler, Michaela; Mettenleiter, Gabriele; Schulz, Michael; Böddrich, Annett; Erck, Christian; Martens, Henrik; Walch, Axel Karl; Madl, Tobias; Wanker, Erich E.; Conrad, Marcus; de Angelis, Martin Hrabě; Reif, Bernd: The redox environment triggers conformational changes and aggregation of hIAPP in Type II Diabetes. Scientific Reports 7 (1), 2017 mehr…