Date of Award

3-1-2024

Thesis Type

masters

Document Type

Thesis (Restricted Access)

Divisions

science

Department

Department of Physics

Institution

Universiti Malaya

Abstract

Beta-pleated amyloid fibrils characterised by distinct beta-sheet conformation are crucial in amyloid diseases by aggregating and depositing in tissues which leading to organ dysfunction. In the case of amyloid disorders, precise fibril identification is paramount for developing effective treatment strategies. This project harnesses Raman spectroscopy, Small Angle X-ray Scattering (SAXS) and X-ray Fluorescence (XRF) to achieve rapid and non-destructive diagnosis of amyloid in human tissues. Biopsy samples from 22 patients were analysed using Raman spectroscopy in a spectral range of 600–1800 cm-1 revealed reliable biomolecular fingerprints of amides, lipids, and side-chain amino acids. Statistical analyses involving Principal Component analysis (PCA) of Raman biomolecular intensities and protein-to-lipid ratios differentiated amyloid from control samples, particularly in amide biomolecules. We used SAXS to look at the differences in peak intensities and structural changes at the cellular level between control and amyloid tissues in q-region range of 0.01–2.00 nm-1. Subsequent statistical analyses highlighted the diversity of amyloid pathology across organs. XRF analysis in the energy range between 0–25 keV identified unique elemental characterisation, including elevated levels of potassium (K) and calcium (Ca), diminished iron (Fe), and the exclusive detection of arsenic (As) in amyloid tissues. These findings extend the characterisation of beta pleated amyloid fibril database and suggest a future with improved amyloid diagnostics.

Note

Dissertation (M.A) – Faculty of Science, Universiti Malaya, 2024.

Additional Files
15758-Nurul_Shahira_Mohd_Nor_Ihsan.pdf (2468 kB)
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