Quantitative morphological analysis reveals ultrastructural diversity of amyloid fibrils from alpha-synuclein mutants.

ABSTRACT: High resolution atomic force microscopy is a powerful tool to characterize nanoscale morphological features of protein amyloid fibrils. Comparison of fibril morphological properties between studies has been hampered by differences in analysis procedures and measurement error determination used by various authors. We describe a fibril morphology analysis method that allows for quantitative comparison of features of amyloid fibrils of any amyloidogenic protein measured by atomic force microscopy. We have used tapping mode atomic force microscopy in liquid to measure the morphology of fibrillar aggregates of human wild-type alpha-synuclein and the disease-related mutants A30P, E46K, and A53T. Analysis of the images shows that fibrillar aggregates formed by E46K alpha-synuclein have a smaller

SUBMITTER: van Raaij ME 

PROVIDER: S-EPMC1635669 | biostudies-literature | 2006 Dec

REPOSITORIES: biostudies-literature