Localization microscopy for the study of amyloid fibril formation

Dorothea Pinotsi; Gabriele S. Kaminski Schierle; Eric Rees; Clemens F. Kaminski

doi:10.1117/12.2022589

20 September 2013 Localization microscopy for the study of amyloid fibril formation

Dorothea Pinotsi, Gabriele S. Kaminski Schierle, Eric Rees, Clemens F. Kaminski

Proceedings Volume 8815, Nanoimaging and Nanospectroscopy; 88150G (2013) https://doi.org/10.1117/12.2022589
Event: SPIE NanoScience + Engineering, 2013, San Diego, California, United States

Abstract

Super-resolution microscopy has emerged as a powerful and non-invasive tool for the study of molecular processes both in vitro, but also as they occur in live cells. Here we present the application of direct stochastic optical reconstruction microscopy (dSTORM), a super-resolution technique based on single molecule localization, to determine the morphology of protein aggregates and of small extra- and intracellular structures. The technique reveals details down to 20 nm providing information on scales much smaller than the wavelength of the probing light. We use dSTORM in the study of amyloid fibril self-assembly processes associated with neurodegenerative diseases, such as Alzheimer's and Parkinson's diseases. We show that the aggregation process can be followed kinetically and observe the emergence of amyloid structures in time as they occur in vitro. As an all optical technique, there is translation potential from studies in vitro to in vivo applications.

Citation Download Citation

Dorothea Pinotsi, Gabriele S. Kaminski Schierle, Eric Rees, and Clemens F. Kaminski "Localization microscopy for the study of amyloid fibril formation", Proc. SPIE 8815, Nanoimaging and Nanospectroscopy, 88150G (20 September 2013); https://doi.org/10.1117/12.2022589

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