Analysis of structural order in amyloid fibrils

摘要

We discuss the application of atomic force microscopy to characterize supra-molecular ordering in elongated protein aggregates such as amyloid fibrils. The measurements reveal that the one-dimensional defect density along these structures is comparable to that found in true three-dimensional macromolecular crystals. The high level of structural order has important implications for understanding the nature of the interactions responsible for protein aggregation, and sheds light on the involvement of amyloid fibrils in aberrant biological pathways.