Buch, Englisch, 149 Seiten, Format (B × H): 160 mm x 241 mm, Gewicht: 3849 g
Reihe: Springer Theses
Buch, Englisch, 149 Seiten, Format (B × H): 160 mm x 241 mm, Gewicht: 3849 g
Reihe: Springer Theses
ISBN: 978-3-319-39533-3
Verlag: Springer International Publishing
Amyloid-ß (Aß) 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 Aß 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.
Zielgruppe
Research
Autoren/Hrsg.
Fachgebiete
- Naturwissenschaften Physik Elektromagnetismus Mikroskopie, Spektroskopie
- Medizin | Veterinärmedizin Medizin | Public Health | Pharmazie | Zahnmedizin Vorklinische Medizin: Grundlagenfächer Molekulare Medizin, Zellbiologie
- Medizin | Veterinärmedizin Medizin | Public Health | Pharmazie | Zahnmedizin Klinische und Innere Medizin Neurologie, Klinische Neurowissenschaft
- Naturwissenschaften Physik Thermodynamik Festkörperphysik, Kondensierte Materie
- Technische Wissenschaften Maschinenbau | Werkstoffkunde Technische Mechanik | Werkstoffkunde Materialwissenschaft: Biomaterialien, Nanomaterialien, Kohlenstoff
- Naturwissenschaften Chemie Analytische Chemie Magnetresonanz
Weitere Infos & Material
Introduction.- Literature Review and Theoretical Concepts.- Experimental Methodology.- Substrate Development of the Imaging of Amyloid Proteins with SPM Methods.- Scanning Probe Microscopy Methods of Imaging Amyloid Peptides During the Aggregation Process.- Spectroscopy and Thermal SPM Methods of Studying Aß1:42.- The Application of Biophysical Techniques to the Study of the Inhibition of Aggregation of Aß Using PINPs Liposomes.- Conclusion and Future Perspectives.