Characterising Interactions Between Amyloid-beta 42 and Amylin Peptide Heterodimers: A Molecular Simulation Approach
Amyloid-beta 42 (Aß42) and amylin are intrinsically disordered peptides. Pathogenic aggregation of peptides results in Alzheimer’s disease (AD) and Type-2 diabetes (T2D), by Aß42 and amylin, respectively. High risk of AD in T2D patients exists due to cross-aggregation in brain. Difficulty in in-vitr...
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| Format: | Thesis |
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Curtin University
2022
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| Online Access: | http://hdl.handle.net/20.500.11937/92792 |
| _version_ | 1848765665417101312 |
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| author | Sonar, Krushna Satish |
| author_facet | Sonar, Krushna Satish |
| author_sort | Sonar, Krushna Satish |
| building | Curtin Institutional Repository |
| collection | Online Access |
| description | Amyloid-beta 42 (Aß42) and amylin are intrinsically disordered peptides. Pathogenic aggregation of peptides results in Alzheimer’s disease (AD) and Type-2 diabetes (T2D), by Aß42 and amylin, respectively. High risk of AD in T2D patients exists due to cross-aggregation in brain. Difficulty in in-vitro characterisation aggregation mechanism elusive. We have managed to shed light on mechanism by sampling conformations and exploiting the hydrophobic nature of peptides using enhanced simulation on monomer (Aß42), Aß42 homo-and heterodimer (Aß42-Amylin). |
| first_indexed | 2025-11-14T11:38:52Z |
| format | Thesis |
| id | curtin-20.500.11937-92792 |
| institution | Curtin University Malaysia |
| institution_category | Local University |
| last_indexed | 2025-11-14T11:38:52Z |
| publishDate | 2022 |
| publisher | Curtin University |
| recordtype | eprints |
| repository_type | Digital Repository |
| spelling | curtin-20.500.11937-927922023-07-20T04:06:23Z Characterising Interactions Between Amyloid-beta 42 and Amylin Peptide Heterodimers: A Molecular Simulation Approach Sonar, Krushna Satish Amyloid-beta 42 (Aß42) and amylin are intrinsically disordered peptides. Pathogenic aggregation of peptides results in Alzheimer’s disease (AD) and Type-2 diabetes (T2D), by Aß42 and amylin, respectively. High risk of AD in T2D patients exists due to cross-aggregation in brain. Difficulty in in-vitro characterisation aggregation mechanism elusive. We have managed to shed light on mechanism by sampling conformations and exploiting the hydrophobic nature of peptides using enhanced simulation on monomer (Aß42), Aß42 homo-and heterodimer (Aß42-Amylin). 2022 Thesis http://hdl.handle.net/20.500.11937/92792 Curtin University restricted |
| spellingShingle | Sonar, Krushna Satish Characterising Interactions Between Amyloid-beta 42 and Amylin Peptide Heterodimers: A Molecular Simulation Approach |
| title | Characterising Interactions Between Amyloid-beta 42
and Amylin Peptide Heterodimers: A Molecular
Simulation Approach |
| title_full | Characterising Interactions Between Amyloid-beta 42
and Amylin Peptide Heterodimers: A Molecular
Simulation Approach |
| title_fullStr | Characterising Interactions Between Amyloid-beta 42
and Amylin Peptide Heterodimers: A Molecular
Simulation Approach |
| title_full_unstemmed | Characterising Interactions Between Amyloid-beta 42
and Amylin Peptide Heterodimers: A Molecular
Simulation Approach |
| title_short | Characterising Interactions Between Amyloid-beta 42
and Amylin Peptide Heterodimers: A Molecular
Simulation Approach |
| title_sort | characterising interactions between amyloid-beta 42
and amylin peptide heterodimers: a molecular
simulation approach |
| url | http://hdl.handle.net/20.500.11937/92792 |