SSPaQ: A Subtractive Segmentation Approach for the Exhaustive Parallel Quantification of the Extent of Protein Modification at Every Possible Site
| العنوان: | SSPaQ: A Subtractive Segmentation Approach for the Exhaustive Parallel Quantification of the Extent of Protein Modification at Every Possible Site |
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| المؤلفون: | Martine Cadene, Guillaume Gabant, Alain Boyer |
| المساهمون: | Centre de biophysique moléculaire (CBM), Université d'Orléans (UO)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie du CNRS (INC) |
| المصدر: | Journal of The American Society for Mass Spectrometry Journal of The American Society for Mass Spectrometry, Springer Verlag (Germany), 2016, 27 (8), pp.1328-1343. ⟨10.1007/s13361-016-1416-y⟩ |
| بيانات النشر: | American Chemical Society (ACS), 2016. |
| سنة النشر: | 2016 |
| مصطلحات موضوعية: | 0301 basic medicine, chemistry.chemical_classification, medicine.diagnostic_test, Chemistry, [SDV]Life Sciences [q-bio], Binding protein, Proteolysis, Peptide, Context (language use), Ligand (biochemistry), Proteomics, Amino acid, 03 medical and health sciences, 030104 developmental biology, Biochemistry, Structural Biology, medicine, Target protein, Spectroscopy |
| الوصف: | International audience; Protein modifications, whether chemically induced or post-translational (PTMs), play an essential role for the biological activity of proteins. Understanding biological processes and alterations thereof will rely on the quantification of these modifications on individual residues. Here we present SSPaQ, a subtractive method for the parallel quantification of the extent of modification at each possible site of a protein. The method combines uniform isotopic labeling and proteolysis with MS, followed by a segmentation approach, a powerful tool to refine the quantification of the degree of modification of a peptide to a segment containing a single modifiable amino acid. The strength of this strategy resides in: (1) quantification of all modifiable sites in a protein without prior knowledge of the type(s) of modified residues; (2) insensitivity to changes in the solubility and ionization efficiency of peptides upon modification; and (3) detection of missed cleavages caused by the modification for mitigation. The SSPaQ method was applied to quantify modifications resulting from the interaction of human phosphatidyl ethanolamine binding protein 1 (hPEBP1), a metastasis suppressor gene product, with locostatin, a covalent ligand and antimigratory compound with demonstrated activity towards hPEBP1. Locostatin is shown to react with several residues of the protein. SSPaQ can more generally be applied to induced modification in the context of drugs that covalently bind their target protein. With an alternate front-end protocol, it could also be applied to the quantification of protein PTMs, provided a removal tool is available for that PTM |
| تدمد: | 1044-0305 |
| URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7957f738a93b2838d98daa927c983e56 https://doi.org/10.1007/s13361-016-1416-y |
| حقوق: | CLOSED |
| رقم الأكسشن: | edsair.doi.dedup.....7957f738a93b2838d98daa927c983e56 |
| قاعدة البيانات: | OpenAIRE |
Find this article in full text from Springer Verlag. 
Find this issue from the American Chemical Society | تدمد: | 10440305 |
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