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Caractérisation structurale de la glycosylation des protéines : de la glycomique à la glycoprotéomique, une stratégie utile pour l’étude des gonadotrophines

Abstract : Polysaccharides from glycoproteins play an important part in numerous biological processes and pathologies. Their structural elucidation requires performant and sensitive tools capable of assessing the heterogeneity of such glycans. Different approaches were developed: N-glycan analysis by MALDI-TOF and LC-ESI-FTMS proteomics.Glycomics is the analysis of glycans independently of their linked-protein and can be using to obtain a glycosylation fingerprint of a protein, fluid etc. Developments of innovative sample and matrix preparation conditions, including glycan chemical modification, improved their mass spectrometry detection and fragmentation.Glycopeptide and glycoprotein analysis permits selective assessment of the glycan population across the protein hence allowing the characterization of molecular microheterogeneity of the different glycoforms. The development and integration of non-specific protease digestion and stepped-energy fragmentation produced more diverse and reliable identifications.Because of their critical role in gestation and embryo development, glycosylated gonadotropins are of major medical and veterinary interest. Combining analytical methodologies granted access to the characterization of population-specific glycosylation motifs.
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Nicolas Eskenazi. Caractérisation structurale de la glycosylation des protéines : de la glycomique à la glycoprotéomique, une stratégie utile pour l’étude des gonadotrophines. Chimie analytique. Université Paris sciences et lettres, 2019. Français. ⟨NNT : 2019PSLET032⟩. ⟨tel-02896596v2⟩

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