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Analyse par spectrométrie de masse des tubulines et de l'hormone de croissance

Abstract : The tubulins are proteins involved in cellular processes that are essential for cell life. The tubulins are polymodified at their C-terminal extremities. Different techniques have been used to characterize the polymodifications of tubulins. However, some challenges remain in the fine identification of some structures. In fact, mass spectrometry ion mobility can separate ions of the same m/z ratio depending on their conformations. In the first part of this thesis, an ion mobility mass spectrometry analysis allowed the separation of two synthetic peptides that mimic the structure of C-terminal peptides of biglycylated α-tubulins. In order to extrapolate this type of experiment to the C-terminal peptides purified from biological tubulins, we employed an analytical process to analyze these peptides from purified brain tubulins. Growth hormone (GH) is an anabolic hormone and a doping agent used by athletes. The availability of rhGH in the black-market has continuously increased because of doping in sports. The natural and the biosynthetic hGH have identical peptidic sequences. So far, the valid hGH anti-doping tests by the world antidoping agency are based on immunological recognition. However, Immunoassays have their own limitations. Therefore, the next generation analysis of GH has to be more specific and accurate. In the second part of this thesis, mass spectrometry coupled to reversed phase chromatography was used to find chemical differences between the pituitary hGH and the rhGH. The pituitary extracted hGH is glycosylated whereas the biotech product is sugar free. The present work represents an opening towards a novel methodology for a novel hGH anti-doping test.
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Hala Dadi. Analyse par spectrométrie de masse des tubulines et de l'hormone de croissance. Chimie analytique. Université Paris Saclay (COmUE), 2018. Français. ⟨NNT : 2018SACLS582⟩. ⟨tel-02560081⟩

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