2017
- The redox environment triggers conformational changes and aggregation of hIAPP in Type II Diabetes. Scientific Reports 7 (1), 2017 mehr…
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:
- Misfolding, aggregation, and cell toxicity of human islet amyloid polypeptide (IAPP).
- Mechanisms of membrane disruption by amyloid-beta (related to Alzheimer's Disease) and IAPP (implicated in type-2 diabetes).
- Atomic-level resolution structures and dynamics of amyloid protein intermediates by NMR.
- Effects of amyloid inhibitors on the structure and toxicity of abeta and IAPP.
Post-doc:
Diana Rodriguez (2015-2017, TUM)