| 書目名稱 | Nanoscale Imaging and Characterisation of Amyloid-β |
| 編輯 | Claire Louisa Tinker-Mill |
| 視頻video | http://file.papertrans.cn/661/660934/660934.mp4 |
| 概述 | Nominated as an outstanding Ph.D. thesis by the Lancaster University, UK.Presents a detailed study of amyloid-beta using multiple methods of atomic force microscopy.Author received the 2012 and 2014 J |
| 叢書名稱 | Springer Theses |
| 圖書封面 |  |
| 描述 | This thesis presents a method for reliably and robustly producing samples of amyloid-β (Aβ) by capturing them at various stages of aggregation, as well as the results of subsequent imaging with various atomic force microscopy (AFM) methods, all of which add value to the data gathered by collecting information on the peptide’s nanomechanical, elastic, thermal or spectroscopical properties.?.Amyloid-β (Aβ) undergoes a hierarchy of aggregation following a structural transition, making it an ideal subject of study using scanning probe microscopy (SPM), dynamic light scattering (DLS) and other physical techniques. By imaging samples of Aβ with Ultrasonic Force Microscopy, a detailed substructure to the morphology is revealed, which correlates well with the most advanced cryo-EM work. Early stage work in the area of thermal and spectroscopical AFM is also presented, and indicates the promise these techniques may hold for imaging sensitive and complex biological materials. This thesis demonstrates that physical techniques can be highly complementary when studying the aggregation of amyloid peptides, and allow the detection of subtle differences in their aggregation processes.. |
| 出版日期 | Book 2016 |
| 關鍵詞 | AFM Imaging of Amyloid-beta; Nanomechanical Characterisation; Alzheimer‘s Disease and AFM; Aggregation |
| 版次 | 1 |
| doi | https://doi.org/10.1007/978-3-319-39534-0 |
| isbn_softcover | 978-3-319-81907-5 |
| isbn_ebook | 978-3-319-39534-0Series ISSN 2190-5053 Series E-ISSN 2190-5061 |
| issn_series | 2190-5053 |
| copyright | Springer International Publishing Switzerland 2016 |
|Archiver|手機版|小黑屋|
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