A Proteomic Analysis of Biological Sex and Health in Gurat, France

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Dolphin, Alexis

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University of Waterloo

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Paleoproteomics, the study of ancient proteins, uses mass spectrometry to identify and characterize proteins by their amino acid sequences. This thesis explores the potential of paleoproteomics to inform bioarchaeological interpretations of biological sex and health in a small medieval population from Gurat, France. Ten milligram enamel samples from six individuals excavated from a rock-cut cave church were analyzed using liquid chromatography-tandem mass spectrometry (LC-MS/MS) to identify proteins in enamel and evaluate their interpretive potential. The primary aim of this project was to test a modified method to investigate its ability to successfully identify amelogenin (amelogenin-X and amelogenin-Y) and immune proteins (C-reactive protein and immunoglobulin-gamma). This method was intentionally modified to reduce analytical costs and resource requirements, while remaining applicable to very small quantities of dental enamel, thereby increasing its feasibility for archaeological and ethically sensitive sampling contexts. The enamel-specific protein amelogenin was successfully identified in all six samples, allowing for proteomic estimations of biological sex to be made. In contrast, one non-enamel-specific immune protein (C-reactive protein) was identified in only one sample, reflecting uncertainty regarding the abundance and preservation of immune proteins in enamel, the immune histories of the Gurat individuals, and the sensitivity of the modified method for immune protein detection. These results highlight both the strengths and limitations of paleoproteomics, offering avenues of exploration in future directions. Above all, this thesis finds that proteomic analyses can complement osteological analyses to offer valuable insight into archaeological populations.

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