Aggregation Inhibition and Detection of Alzheimer’s Amyloidogenic and Oligomeric Peptides

• Other Authors: Elbassal, Esmail A. E. (author)
• Format: Others
• Language: English
• Published: Florida Atlantic University
• Subjects: Alzheimer's disease; Amyloid beta-protein; Oligomers; Protein Aggregates; Neurodegenerative Diseases
• Online Access: http://purl.flvc.org/fau/fd/FA00013009

Protein aggregation, oligomer and fibril formation is one of the dominant characteristics in the pathogenesis of a number of neurodegenerative diseases, such as Alzheimer’s disease (AD). Inhibition of toxic oligomer and fibril formation is one of the approaches to find potential drug candidates for AD. Additionally, early diagnosis of these amyloid species can provide mechanistic understanding of protein aggregation and thus can pave the way for preventing the onset of AD. The aim of this dissertation was 1) to explore the effects of charged cholesterol derivatives on the aggregation kinetic behavior of Amyloid-β40 (Aβ40), 2) to probe Aβ40 oligomer and amyloid formation in vitro using gold nanoparticles (AuNPs), and 3) to monitor the kinetic effect of various natural product molecules on Aβ40 aggregation in vitro. In the first chapter, a general introduction about AD as an amyloidogenic disease, amyloid cascade hypothesis, and the manipulation of Aβ peptides aggregation kinetics using different approaches was presented. In the second chapter, we studied the effects of oppositely charged cholesterol derivatives on the aggregation kinetics of Aβ. In the third chapter, we developed a gold nanoparticles (AuNPs) assay to probe Aβ40 oligomers and amyloid formation. In chapter IV, we monitored the effects of various small molecules on the aggregation kinetics of Aβ40. In chapter V, we discussed the methods and experimental details. === Includes bibliography. === Dissertation (Ph.D.)--Florida Atlantic University, 2018. === FAU Electronic Theses and Dissertations Collection