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Understanding secondary nucleation of the amyloid β peptide

Thacker, Dev LU (2022)
Abstract
Alzheimer’s Disease (AD) is a devastating neurodegenerative disease associated with massive neuronal cell death during its pathology. The involvement of the amyloid β 42 (Aβ42) peptide
and its role in neurotoxicity is now well established. It is known that the production of oligomers during the aggregation of Aβ42 into highly ordered fibrils is responsible for neuronal cell death. However, the efforts in finding a cure have been greatly hindered because of the lack of understanding of the molecular mechanisms of Aβ42 aggregation. This thesis focuses on understanding the molecular mechanism of secondary nucleation, the process which is most prolific in the production of oligomers. In particular, the work focuses on intrinsic
factors... (More)
Alzheimer’s Disease (AD) is a devastating neurodegenerative disease associated with massive neuronal cell death during its pathology. The involvement of the amyloid β 42 (Aβ42) peptide
and its role in neurotoxicity is now well established. It is known that the production of oligomers during the aggregation of Aβ42 into highly ordered fibrils is responsible for neuronal cell death. However, the efforts in finding a cure have been greatly hindered because of the lack of understanding of the molecular mechanisms of Aβ42 aggregation. This thesis focuses on understanding the molecular mechanism of secondary nucleation, the process which is most prolific in the production of oligomers. In particular, the work focuses on intrinsic
factors affecting secondary nucleation such as hydrophobic residues and surfaces on the fibrils, which catalyze the aggregation of monomers during secondary nucleation. We also show the possibility of molecular specificity being involved in secondary nucleation, and open avenues of further studies that will help understand the molecular mechanism of this phenomenon. (Less)
Please use this url to cite or link to this publication:
author
supervisor
opponent
  • Professor Serpell, Louise, University of Sussex
organization
publishing date
type
Thesis
publication status
published
subject
keywords
Alzheimer's disease (AD), A beta 1-42, Amyloid aggregation, secondary nucleation
pages
194 pages
publisher
Lund University
defense location
Kemicentrum: A, Lund
defense date
2022-03-09 09:15:00
ISBN
978-91-7422-860-1
978-91-7422-861-8
language
English
LU publication?
yes
id
37c60125-6434-4de0-bcf5-337534393f74
date added to LUP
2022-02-08 14:41:47
date last changed
2022-02-09 15:26:36
@phdthesis{37c60125-6434-4de0-bcf5-337534393f74,
  abstract     = {{Alzheimer’s Disease (AD) is a devastating neurodegenerative disease associated with massive neuronal cell death during its pathology. The involvement of the amyloid β 42 (Aβ42) peptide<br/>and its role in neurotoxicity is now well established. It is known that the production of oligomers during the aggregation of Aβ42 into highly ordered fibrils is responsible for neuronal cell death. However, the efforts in finding a cure have been greatly hindered because of the lack of understanding of the molecular mechanisms of Aβ42 aggregation. This thesis focuses on understanding the molecular mechanism of secondary nucleation, the process which is most prolific in the production of oligomers. In particular, the work focuses on intrinsic<br/>factors affecting secondary nucleation such as hydrophobic residues and surfaces on the fibrils, which catalyze the aggregation of monomers during secondary nucleation. We also show the possibility of molecular specificity being involved in secondary nucleation, and open avenues of further studies that will help understand the molecular mechanism of this phenomenon.}},
  author       = {{Thacker, Dev}},
  isbn         = {{978-91-7422-860-1}},
  keywords     = {{Alzheimer's disease (AD); A beta 1-42; Amyloid aggregation; secondary nucleation}},
  language     = {{eng}},
  month        = {{02}},
  publisher    = {{Lund University}},
  school       = {{Lund University}},
  title        = {{Understanding secondary nucleation of the amyloid β peptide}},
  year         = {{2022}},
}