Ihsan, N. S. Mohd Nor and Abdul Sani, S. F. and Looi, L. M. and Cheah, P. L. and Chiew, S. F. and Pathmanathan, Dharini and Bradley, D. A. (2023) A review: Exploring the metabolic and structural characterisation of beta pleated amyloid fibril in human tissue using Raman spectrometry and SAXS. Progress in Biophysics & Molecular Biology, 182. pp. 59-74. ISSN 0079-6107, DOI https://doi.org/10.1016/j.pbiomolbio.2023.06.002.
Full text not available from this repository.Abstract
Amyloidosis is a deleterious condition caused by abnormal amyloid fibril build-up in living tissues. To date, 42 proteins that are linked to amyloid fibrils have been discovered. Amyloid fibril structure variation can affect the severity, progression rate, or clinical symptoms of amyloidosis. Since amyloid fibril build-up is the primary pathological basis for various neurodegenerative illnesses, characterization of these deadly proteins, particularly utilising optical techniques have been a focus. Spectroscopy techniques provide significant non-invasive platforms for the investigation of the structure and conformation of amyloid fibrils, offering a wide spectrum of analyses ranging from nanometric to micrometric size scales. Even though this area of study has been intensively explored, there still remain aspects of amyloid fibrillization that are not fully known, a matter hindering progress in treating and curing amyloidosis. This review aims to provide recent updates and comprehensive information on optical techniques for metabolic and proteomic characterization of beta-pleated amyloid fibrils found in human tissue with thorough literature analysis of publications. Raman spectroscopy and SAXS are well established experimental methods for study of structural properties of biomaterials. With suitable models, they offer extended information for valid proteomic analysis under physiologically relevant conditions. This review points to evidence that despite limitations, these techniques are able to provide for the necessary output and proteomics indication in order to extrapolate the aetiology of amyloid fibrils for reliable diagnostic purposes. Our metabolic database may also contribute to elucidating the nature and function of the amyloid proteome in development and clearance of amyloid diseases.
| Item Type: | Article |
|---|---|
| Funders: | Fundamental Research Grant Scheme (FRGS) of the Ministry of Educa-tion [Grant o: Malaysia-FRGS/1/2020/STG05/UM/02/5] |
| Uncontrolled Keywords: | Amyloid fibril tissue; beta-pleated amyloid; Optical diagnostic; Raman spectroscopy; SAXS; Metabolite database |
| Subjects: | Q Science > QC Physics Q Science > QD Chemistry |
| Divisions: | Faculty of Science > Department of Physics |
| Depositing User: | Ms. Juhaida Abd Rahim |
| Date Deposited: | 11 Oct 2025 04:35 |
| Last Modified: | 11 Oct 2025 04:35 |
| URI: | http://eprints.um.edu.my/id/eprint/48239 |
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