Optical Super-Resolution Imaging of beta-Amyloid Aggregation In Vitro and In Vivo: Method and Techniques. Pinotsi, D., Kaminski Schierle, G., S., & Kaminski, C., F. Systems Biology of Alzheimer's Disease, 1303:125-141, Springer New York, 2016. ![Optical Super-Resolution Imaging of beta-Amyloid Aggregation In Vitro and In Vivo: Method and Techniques [pdf]](https://bibbase.org/img/filetypes/pdf.svg "pdf")
Paper abstract bibtex Super-resolution microscopy has emerged as a powerful and non-invasive tool for the study of molecular processes both in vitro and in live cells. In particular, super-resolution microscopy has proven valuable for research studies in protein aggregation. In this chapter we present details of recent advances in this method and the specifi c techniques, enabling the study of amyloid beta aggregation optically, both in vitro and in cells. First, we show that variants of optical super-resolution microscopy provide a capability to visualize oligomeric and fi brillar structures directly, providing detailed information on species morphology in vitro and even in situ, in the cellular environment. We focus on direct Stochastic Optical Reconstruction Microscopy, d STORM, which provides morphological detail on spatial scales below 20 nm, and provide detailed protocols for its implementation in the context of amyloid beta research. Secondly, we present a range of optical techniques that offer super-resolution indirectly, which we call multi-parametric micros-copy. The latter offers molecular scale information on self-assembly reactions via changes in protein or fl uorophore spectral signatures. These techniques are empowered by our recent discovery that disease related amyloid proteins adopt intrinsic energy states upon fi brilisation. We show that fl uorescence lifetime imaging provides a particularly sensitive readout to report on the aggregation state, which is robustly quantifi able for experiments performed either in vitro or in vivo.
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abstract = {Super-resolution microscopy has emerged as a powerful and non-invasive tool for the study of molecular processes both in vitro and in live cells. In particular, super-resolution microscopy has proven valuable for research studies in protein aggregation. In this chapter we present details of recent advances in this method and the specifi c techniques, enabling the study of amyloid beta aggregation optically, both in vitro and in cells. First, we show that variants of optical super-resolution microscopy provide a capability to visualize oligomeric and fi brillar structures directly, providing detailed information on species morphology in vitro and even in situ, in the cellular environment. We focus on direct Stochastic Optical Reconstruction Microscopy, d STORM, which provides morphological detail on spatial scales below 20 nm, and provide detailed protocols for its implementation in the context of amyloid beta research. Secondly, we present a range of optical techniques that offer super-resolution indirectly, which we call multi-parametric micros-copy. The latter offers molecular scale information on self-assembly reactions via changes in protein or fl uorophore spectral signatures. These techniques are empowered by our recent discovery that disease related amyloid proteins adopt intrinsic energy states upon fi brilisation. We show that fl uorescence lifetime imaging provides a particularly sensitive readout to report on the aggregation state, which is robustly quantifi able for experiments performed either in vitro or in vivo.},
bibtype = {article},
author = {Pinotsi, Dorothea and Kaminski Schierle, Gabriele S and Kaminski, Clemens F},
journal = {Systems Biology of Alzheimer's Disease}
}
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