Identifying Polymorphs of Amyloid-β (1–40) Fibrils Using High-Resolution Atomic Force Microscopy
2019
Lin, Yi-Chih | Komatsu, Hiroaki | Ma, Jianqiang | Axelsen, Paul H. | Fakhraai, Zahra
Many amyloid-β fibril preparations are highly polymorphic, and the conditions under which they are formed determine their morphology. This report describes the application of high-resolution atomic force microscopy (HR-AFM), combined with volume-per-length analysis, to define, identify, and quantify the structural components of polymorphic Aβ fibril preparations. Volume-per-length analysis confirms that they are composed of discrete cross-β filaments, and the analysis of HR-AFM images yields the number of striations in each fibril. Compared to mass-per-length analysis by electron microscopy, HR-AFM analysis yields narrower distributions, facilitating rapid and label-free quantitative morphological characterization of Aβ fibril preparations.
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