Structural evaluation of an amyloid fibril model using small-angle x-ray scattering
| Autor: | Ashwinkumar A. Bhirde, Mina Choi, Eshan Dahal, Serge L. Beaucage, Nadia Alam, Aldo Badano |
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| Rok vydání: | 2017 |
| Předmět: |
0301 basic medicine
Amyloid Time Factors Biophysics macromolecular substances Protein aggregation Fibril Models Biological Absorbance 03 medical and health sciences chemistry.chemical_compound X-Ray Diffraction Dynamic light scattering Structural Biology Scattering Small Angle Bovine serum albumin Molecular Biology biology Scattering Small-angle X-ray scattering fungi Serum Albumin Bovine Cell Biology Dynamic Light Scattering Congo red 030104 developmental biology chemistry biology.protein |
| Zdroj: | Physical Biology. 14:046001 |
| ISSN: | 1478-3975 |
| Popis: | Amyloid fibrils are highly structured protein aggregates associated with a wide range of diseases including Alzheimer's and Parkinson's. We report a structural investigation of an amyloid fibril model prepared from a commonly used plasma protein (bovine serum albumin (BSA)) using small-angle x-ray scattering (SAXS) technique. As a reference, the size estimates from SAXS are compared to dynamic light scattering (DLS) data and the presence of amyloid-like fibrils is confirmed using Congo red absorbance assay. Our SAXS results consistently show the structural transformation of BSA from spheroid to rod-like elongated structures during the fibril formation process. We observe the elongation of fibrils over two months with fibril length growing from 35.9 ± 3.0 nm to 51.5 ± 2.1 nm. Structurally metastable fibrils with distinct SAXS profiles have been identified. As proof of concept, we demonstrate the use of such distinct SAXS profiles to detect fibrils in the mixture solutions of two species by estimating their volume fractions. This easily detectable and well-characterized amyloid fibril model from BSA can be readily used as a control or standard reference to further investigate SAXS applications in the detection of structurally diverse amyloid fibrils associated with protein aggregation diseases. |
| Databáze: | OpenAIRE |
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