Aggregation kinetics of A\U+fffd\ peptides and the inhibition effects of small molecules on A\U+fffd\ peptide aggregation
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 o...
Other Authors: | |
---|---|
Format: | Others |
Language: | English |
Published: |
Florida Atlantic University
|
Subjects: | |
Online Access: | http://purl.flvc.org/FAU/3358550 |
id |
ndltd-fau.edu-oai-fau.digital.flvc.org-fau_4020 |
---|---|
record_format |
oai_dc |
spelling |
ndltd-fau.edu-oai-fau.digital.flvc.org-fau_40202019-07-04T03:51:03Z Aggregation kinetics of A\U+fffd\ peptides and the inhibition effects of small molecules on A\U+fffd\ peptide aggregation Hijazi, Ahmad Alex. Text Electronic Thesis or Dissertation Florida Atlantic University English x, 62 p. : ill. (some col.) electronic 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. by Ahmad Alex Hijazi. Thesis (M.S.)--Florida Atlantic University, 2012. Includes bibliography. Mode of access: World Wide Web. System requirements: Adobe Reader. Amyloid beta-protein Proteins--Metabolism--Disorders Prions Alzheimer's disease http://purl.flvc.org/FAU/3358550 829393497 3358550 FADT3358550 fau:4020 Charles E. Schmidt College of Science Department of Chemistry and Biochemistry http://rightsstatements.org/vocab/InC/1.0/ https://fau.digital.flvc.org/islandora/object/fau%3A4020/datastream/TN/view/Aggregation%20kinetics%20of%20A%5CU%2Bfffd%5C%20peptides%20and%20the%20inhibition%20effects%20of%20small%20molecules%20on%20A%5CU%2Bfffd%5C%20peptide%20aggregation.jpg |
collection |
NDLTD |
language |
English |
format |
Others
|
sources |
NDLTD |
topic |
Amyloid beta-protein Proteins--Metabolism--Disorders Prions Alzheimer's disease |
spellingShingle |
Amyloid beta-protein Proteins--Metabolism--Disorders Prions Alzheimer's disease Aggregation kinetics of A\U+fffd\ peptides and the inhibition effects of small molecules on A\U+fffd\ peptide aggregation |
description |
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. === by Ahmad Alex Hijazi. === Thesis (M.S.)--Florida Atlantic University, 2012. === Includes bibliography. === Mode of access: World Wide Web. === System requirements: Adobe Reader. |
author2 |
Hijazi, Ahmad Alex. |
author_facet |
Hijazi, Ahmad Alex. |
title |
Aggregation kinetics of A\U+fffd\ peptides and the inhibition effects of small molecules on A\U+fffd\ peptide aggregation |
title_short |
Aggregation kinetics of A\U+fffd\ peptides and the inhibition effects of small molecules on A\U+fffd\ peptide aggregation |
title_full |
Aggregation kinetics of A\U+fffd\ peptides and the inhibition effects of small molecules on A\U+fffd\ peptide aggregation |
title_fullStr |
Aggregation kinetics of A\U+fffd\ peptides and the inhibition effects of small molecules on A\U+fffd\ peptide aggregation |
title_full_unstemmed |
Aggregation kinetics of A\U+fffd\ peptides and the inhibition effects of small molecules on A\U+fffd\ peptide aggregation |
title_sort |
aggregation kinetics of a\u+fffd\ peptides and the inhibition effects of small molecules on a\u+fffd\ peptide aggregation |
publisher |
Florida Atlantic University |
url |
http://purl.flvc.org/FAU/3358550 |
_version_ |
1719218937263030272 |