Date of Award
2012
Document Type
Thesis
Publication Status
Version of Record
Submission Date
October 2026
Abstract
The pathology of Alzheimer's disease (AD) remains elusive. Competing evidence links amylois \U+fffd\-peptide (A\U+fffd\) amyloid formation to the phenotype of AD (1). The mechanism of amyloid fibril formation has been an ongoing investigation for many years. A\U+fffd\10-23 peptide, a fragment of A\U+fffd\1-42 peptide, contained crucial hydrophobic core residues (2). In this study, an investigation was launched to study the aggreagation process of A\U+fffd\1023 peptide and its ability to form amyloid fibrils. Furthermore, the presence of its hydrophobic core showed importance for its ability to aggregate and form amyloid fibrils. Thereafter, the inhibition of A\U+fffd\1-42 peptide aggregation was studied by using pyrimidine-based compounds. A\U+fffd\1-42 peptides, known to be neurotoxic, aggregate to form amyloid fibrils (3). This investigation may provide insight into the development of novel small molecular candidates to treat AD.
Extent
x, 62 p. : ill. (some col.)
Recommended Citation
Hijazi, Ahmad Alex, "Aggregation kinetics of A\U+fffd\ peptides and the inhibition effects of small molecules on A\U+fffd\ peptide aggregation" (2012). Electronic Theses and Dissertations 2010 - 2019. 446.
https://digitalcommons.fau.edu/etd_general_6/446
Identifier
FADT3358550
Comments
by Ahmad Alex Hijazi.|Thesis (M.S.)--Florida Atlantic University, 2012.|Includes bibliography.|Mode of access: World Wide Web.|System requirements: Adobe Reader.|by Ahmad Alex Hijazi.