A study of the elongation of fibrils of the Alzheimer's amyloid beta protein with a coarse-grained force field

Alzheimer’s disease (AD) is a brain disorder named after the German psychiatrist Alois Alzheimer, who first described the disease in 1906. AD is a form of dementia, characterized by impairment of memory and other intellectual abilities, caused by the loss of neurons and synapses (the structures that permit communication between neurons) in certain regions of the brain. Although the mechanism by which neurons are affected is not yet well understood, research points to a small protein, the beta-amyloid peptide (Abeta), as the first suspect. Ab chains are present in the brains of healthy individuals, but in AD patients, they associate and form clumps that deposit outside neurons, and are believed to trigger the disease. In this dissertation, I use computational methods to study the behavior of the structures formed by Ab chains, when they associate with each other, and how these structures grow. The goal of this work is to use computational methods to complement experimental results by filling the gaps about structural and association mechanism that cannot be accessed by experiments.

Name thesis:degree_name

Doctor of Philosophy (PhD)

Level thesis:degree_level

Dissertation

Discipline thesis:degree_discipline

Physical Sciences and Mathematics

Grantor

Physics and Astronomy

Year dc:date.available

2010

Author dc:creator

• Rojas, Ana

• protein folding
• misfolding disease
• molecular dynamics
• simulations

Statement dc:rights

• unrestricted
• Release the entire work immediately for access worldwide.

Identifier

etd-08162010-102550
https://repository.lsu.edu/gradschool_dissertations/351

OAI identifier oai:identifier

oai:repository.lsu.edu:gradschool_dissertations-1350