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University of Arkansas

Field Amplified Sample Stacking on Amyloid Beta (1-42) Oligomers using Capillary Electrophoresis

Abstract

dc:description.abstract

<p>According to recent literature, it is believed that the oligomeric form of amyloid beta (Aβ) is the leading cause of Alzheimer’s disease (1; 8; 10; 12-18). Additionally, recent studies have eluded to the impact of Alzheimer’s disease (AD) both economically and Socially in today’s society where an increase of about 71% of AD related deaths were recorded between 2000 and 2013 (7). Since the oligomeric forms of Aβ vary in size, shape and some believe conformation, it is vital to utilize a separation technique, such as capilllary electrophoresis (CE) to further understand Aβ aggregation. By understanding Aβ aggregation, treatment of AD or preventive care measurements could be additionally developed.</p> <p>Therefore in this study, field amplified sample stacking (FASS) technique on the CE was utilized to provide higher resolution in oligomeric Aβ1-42 detection without causing significant changes to the aggregation. It was observed that the FASS technique provided smaller peak widths and increased peak heights on the CE compared to the non-FASS conditions. Furthermore by conducting thioflavin-t (ThT) assays, it was observed changing the buffer concentrations in accordance to the FASS technique conditions did not effect the overall aggregation. Thioflavin-t (ThT) assays were also conducted in order to determine an agitation rate where the oligomers of Aβ1-42 were observed on the CE.</p> <p>The oligomeric species observed were believed to be less than or equal to 100 kDa. Additionally, Congo red and Orange G inhibition were conducted to confirm oligomeric Aβ1-42 species were observed on the CE. Both inhibition studies alongside TEM imaging proved the aggregates observed on the CE in the 27 hour aggregation were smaller than proto-fibrils. Future work on natural compound inhibition studies using CE are recommended to see how those inhibitors target Aβ1-42 species that are less than or equal to 100 kDa.</p>

Degree

thesis:*
Name thesis:degree_name
Master of Science in Chemical Engineering (MSChE)
Level thesis:degree_level
Thesis
Year dc:date.available
2015

Author and committee

dc:creator, dc:contributor.*
Author dc:creator
  • Paracha, Sadia Ali
Advisor dc:contributor.advisor
  • Hestekin, Christa N.
Contributors dc:contributor
  • Beitle, Robert R. Jr.
  • Sakon, Joshua

Subjects

dc:subject × 7

Identifiers

dc:identifier.*
Repository record dc:identifier
https://scholarworks.uark.edu/etd/1388
OAI identifier oai:identifier
oai:scholarworks.uark.edu:etd-2387

Chain of custody

source
Harvested from
University of Arkansas
Base URL
scholarworks.uark.edu/do/oai/
Last updated
2026-07-24
Source record
OAI-PMH GetRecord
citation

Paracha, Sadia Ali. Field Amplified Sample Stacking on Amyloid Beta (1-42) Oligomers using Capillary Electrophoresis. Thesis thesis, 2015. https://scholarworks.uark.edu/etd/1388