Understanding amyloid aggregation by statistical analysis of atomic force microscopy images

作者：Adamcik Jozef^*; Jung Jin Mi; Flakowski Jerome; De Los Rios Paolo; Dietler Giovanni; Mezzenga Raffaele

来源：Nature Nanotechnology, 2010, 5(6): 423-428.

DOI：10.1038/NNANO.2010.59

The aggregation of proteins is central to many aspects of daily life, including food processing, blood coagulation, eye cataract formation disease and prion-related neurodegenerative infections(1-5). However, the physical mechanisms responsible for amyloidosis-the irreversible fibril formation of various proteins that is linked to disorders such as Alzheimer's, Creutzfeldt-Jakob and Huntington's diseases-have not yet been fully elucidated(6-9). Here, we show that different stages of amyloid aggregation can be examined by performing a statistical polymer physics analysis of single-molecule atomic force microscopy images of heat-denatured beta-lactoglobulin fibrils. The atomic force microscopy analysis, supported by theoretical arguments, reveals that the fibrils have a multistranded helical shape with twisted ribbon-like structures. Our results also indicate a possible general model for amyloid fibril assembly and illustrate the potential of this approach for investigating fibrillar systems.

• 出版日期2010-6