2017 Participants
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NAME: Mary Bunten

 Cytochrome C Vulnerability to Malondialdehyde (MDA) Modification: A Study Focusing on Mass Spectrometry

This project will investigate the reactivity of malondialdehyde (MDA) with cytochrome c (CYT-C), one of the main proteins of the mitochondrial electron transport chain system. Knowledge gained from this study will offer new insights about the role that MDA might play in diseases such as diabetes where oxidative stress has been implicated with higher levels of MDA in vivo. Several incubations will be performed in order to ascertain the reactivity of MDA with CYT-C at physiological conditions. The goal of this study is threefold. First, to show that the incubation of MDA with cytochrome c under physiological conditions of temperature and pH over time can yield advanced glycation-like end products (AGLEs); compounds previously demonstrated to contribute to many of the chronic complications of diabetes. Second, to characterize the AGLEs of CYT-C using methods such as UV/Visible spectrometry, HPLC, and fluorescence spectroscopy. Third, to study the changes in the structure, amino acid modification, and kinetics of CYT-C with MDA utilizing circular dichroism spectroscopy and MALDI-TOF mass spectrometry.  At present, there is little information about the role of MDA in mitochondrial aging, and specifically, about how MDA affects the structure and function of the electron chain proteins.  Additionally, there have been no studies linking mitochondrial dysfunction with time in presence of MDA which is produced in vivo from fatty acid peroxidation.