Journal article

How is protein aggregation in amyloidogenic diseases modulated by biological membranes?

Christopher Aisenbrey, Tomasz Borowik, Roberth Bystrom, Marcus Bokvist, Fredrick Lindstrom, Hanna Misiak, Marc-Antoine Sani, Gerhard Grobner

EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS | SPRINGER | Published : 2008

Abstract

The fate of proteins with amyloidogenic properties depends critically on their immediate biochemical environment. However, the role of biological interfaces such as membrane surfaces, as promoters of pathological aggregation of amyloidogenic proteins, is rarely studied and only established for the amyloid-beta protein (A beta) involved in Alzheimer's disease, and alpha-synuclein in Parkinsonism. The occurrence of binding and misfolding of these proteins on membrane surfaces, is poorly understood, not at least due to the two-dimensional character of this event. Clearly, the nature of the folding pathway for A beta protein adsorbed upon two-dimensional aggregation templates, must be fundamenta..

View full abstract

University of Melbourne Researchers