Abstract
Amyloids are insoluble, thread-like protein aggregates which are associated with a number of severe diseases. Different techniques currently employed to characterize the structural features of amyloids, such as optical methods, electron microscopy, X-ray diffraction, nuclear magnetic resonance and atomic force microscopy (AFM), are briefly described in the first part of this chapter. Among these techniques, AFM plays a relevant role, as it is capable of imaging samples in different environments without requiring particular preparation, such as staining or fixation procedures. It allows the different steps of the aggregation process to be followed, from early oligomers to fibrils, providing nanometric details of their morphology. AFM has been used to probe the effects of organic and inorganic surfaces on the aggregation process and the interaction of amyloid with model membranes. Finally we review how the statistical analysis of AFM images and force spectroscopymeasurements can give quantitative information on mechanical properties of fibrils.
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Relini, A., Cavalleri, O., Canale, C., Svaldo-Lanero, T., Rolandi, R., Gliozzi, A. (2008). What Can Atomic Force Microscopy Say About Amyloid Aggregates?. In: Tomitori, M., Bhushan, B., Fuchs, H. (eds) Applied Scanning Probe Methods IX. Nano Science and Technolgy. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-540-74083-4_8
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