Roberth Byström, Christopher Aisenbrey, Tomasz Borowik, Marcus Bokvist, Fredrick Lindström, Marc-Antoine Sani, Anders Olofsson, Gerhard Gröbner
Aberrant folded proteins and peptides are hallmarks of amyloidogenic diseases. However, the molecular processes that cause these proteins to adopt non-native structures in vivo and become cytotoxic are still largely unknown, despite intense efforts to establish a general molecular description of their behavior. Clearly, the fate of these proteins is ultimately linked to their immediate biochemical environment in vivo. In this review, we focus on the role of biological membranes, reactive interfaces that not only affect the conformational stability of amyloidogenic proteins, but also their aggregation rates and, probably, their toxicity...
2008: Cell Biochemistry and Biophysics