Albu, Titus; Lee, John P.; Gaudin, Timothy
University of Tennessee at Chattanooga
Place of Publication
Amyloidosis, which involves the precipitation of mis-folded protein aggregates, is a prominent process that occurs in many neurodegenerative conditions such as Alzheimer's disease and Parkinson's disease; the protein aggregates being amyloid-β for Alzheimer’s disease and α-synuclein for Parkinson’s disease. This study has focused on lysozyme modifications induced by metabolites of the commonly found pollutants known as polycyclic aromatic hydrocarbons (PAHs). PAHs are found in substances ranging from grilled meats to cigarette smoke to cosmetics, and they can be metabolized into a family of biological toxins known as benzoquinones. The molecules of interest for this study were 1,4-benzoquinone (pBQ), 2-chloro-1,4-benzoquinone (CBQ), and 2-methyl-1,4- benzoquinone (MBQ). The effect these benzoquinones had on lysozyme was studied by first creating samples through time- and concentration-dependent incubations in physiologic conditions. These samples were then examined through SDS-PAGE analysis, fluorescence assays, and UV-Vis spectroscopy to determine the products created through this modification. Our findings revealed the effective oligomerization and aggregation of lysozyme modified by benzoquinones.
The Grote Chemistry Fund Provost Student Research Award
B. S.; An honors thesis submitted to the faculty of the University of Tennessee at Chattanooga in partial fulfillment of the requirements of the degree of Bachelor of Science.
Amyloidosis; Nervous system -- Degeneration
Greve, Hendrik J., "Modifications of lysozyme by substituted benzoquinones" (2015). Honors Theses.