Karlie Cummins Lewis University, Rachel Lullo Lewis University, Dina Nashed Lewis University
Faculty Sponsor(s): Daniel Kissel Lewis University, Mallory Havens Lewis UniversityAlzheimer’s Disease (AD) is an irreversible neurodegenerative disease that causes a decline in various cognitive abilities including memory loss and an inability to perform simple tasks. The protein amyloid beta (Aβ) is a biomarker utilized to track the progression of the disease as the protein aggregates in the brain due to misfolding. The 42 amino acid sequence results from cleavage of a precursor protein (APP) which aggregates to form beta sheets during post-translational modification as a result of oxidative stress in the brain. The interaction between Aβ-42 and heavy metals such as Cu2+ at the 13th and 14th histidine residues in the primary structure of Aβ-42 enhance the toxicity of the peptide causing the formation of amyloid plaques. The work presented herein focuses on correlating different in vitro techniques to monitor Aβ-42 aggregation under different conditions. Gel electrophoresis was done in the presence of varying concentrations of Cu2+ and copper chelating compounds to quantitatively analyze amyloid peptide aggregation. In addition, microscopy imaging was used to qualitatively study aggregate size and morphology. These results were correlated to determine the effect of Cu2+ and copper coordination compounds on peptide aggregation.
When & Where
Irwin Library 1st Floor