Abstract
Here, we report a study of ex vivo amyloid fibrils formed, respectively, by the Leu174Ser Apolipoprotein A-I (ApoA-I-LS) variant and by β2-microglobulin (β2-m) (Relini et al., J. Biol. Chem. 281:16521–16529, 2006; Relini et al., Biochim. Biophys. Acta 1690:33–41, 2004). In the work on ApoA-I-LS, the AFM has been used to characterize and compare the morphologies of amyloid fibrils isolated from two different patients, while in the study on β2-m our investigation provided important information about the factors that can promote the aggregation in vivo.
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Acknowledgment
We thank Vittorio Bellotti and Giampaolo Merlini (Department of Biochemistry, University of Pavia -Laboratori di Biotecnologie IRCCS Policlinico San Matteo, 27100 Pavia, Italy) for extraction and purification of Apo-A-I and beta2-m ex-vivo amyloid fibrils and expression and purification of recombinant beta2-m.
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Canale, C., Relini, A., Gliozzi, A. (2011). Atomic Force Microscopy of Ex Vivo Amyloid Fibrils. In: Braga, P., Ricci, D. (eds) Atomic Force Microscopy in Biomedical Research. Methods in Molecular Biology, vol 736. Humana Press. https://doi.org/10.1007/978-1-61779-105-5_6
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DOI: https://doi.org/10.1007/978-1-61779-105-5_6
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