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On the utility of predictive chromatography to complement mass spectrometry based intact protein identification

Pridatchenko, Marina ; Perlova, Tatyana ; Ben Hamidane, Hisham ; Goloborodko, Anton ; Tarasova, Irina ; Gorshkov, Alexander ; Evreinov, Victor ; Tsybin, Yury ; Gorshkov, Mikhail

In: Analytical and Bioanalytical Chemistry, 2012, vol. 402, no. 8, p. 2521-2529

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    Titre
    • On the utility of predictive chromatography to complement mass spectrometry based intact protein identification
    Auteur
    • Pridatchenko, Marina. Institute for Energy Problems of Chemical Physics, Russian Academy of Sciences, 119991, Moscow, Russia
    • Perlova, Tatyana. Institute for Energy Problems of Chemical Physics, Russian Academy of Sciences, 119991, Moscow, Russia
    • Ben Hamidane, Hisham. Ecole Polytechnique Federale de Lausanne, 1015, Lausanne, Switzerland
    • Goloborodko, Anton. Institute for Energy Problems of Chemical Physics, Russian Academy of Sciences, 119991, Moscow, Russia
    • Tarasova, Irina. Institute for Energy Problems of Chemical Physics, Russian Academy of Sciences, 119991, Moscow, Russia
    • Gorshkov, Alexander. Institute of Chemical Physics, Russian Academy of Sciences, 119991, Moscow, Russia
    • Evreinov, Victor. Institute of Chemical Physics, Russian Academy of Sciences, 119991, Moscow, Russia
    • Tsybin, Yury. Ecole Polytechnique Federale de Lausanne, 1015, Lausanne, Switzerland
    • Gorshkov, Mikhail. Institute for Energy Problems of Chemical Physics, Russian Academy of Sciences, 119991, Moscow, Russia
    Type de document
    • Postprint
    Langue
    • Anglais
    Publié dans
    • Analytical and Bioanalytical Chemistry, 2012, vol. 402, no. 8, p. 2521-2529. Springer-Verlag
    Autre version électronique
    Identifiant OAI-PMH
    • oai:doc.rero.ch:313853
    Summary
    The amino acid sequence determines the individual protein three-dimensional structure and its functioning in an organism. Therefore, "reading” a protein sequence and determining its changes due to mutations or post-translational modifications is one of the objectives of proteomic experiments. The commonly utilized approach is gradient high-performance liquid chromatography (HPLC) in combination with tandem mass spectrometry. While serving as a way to simplify the protein mixture, the liquid chromatography may be an additional analytical tool providing complementary information about the protein structure. Previous attempts to develop "predictive” HPLC for large biomacromolecules were limited by empirically derived equations based purely on the adsorption mechanisms of the retention and applicable to relatively small polypeptide molecules. A mechanism of the large biomacromolecule retention in reversed-phase gradient HPLC was described recently in thermodynamics terms by the analytical model of liquid chromatography at critical conditions (BioLCCC). In this work, we applied the BioLCCC model to predict retention of the intact proteins as well as their large proteolytic peptides separated under different HPLC conditions. The specific aim of these proof-of-principle studies was to demonstrate the feasibility of using "predictive” HPLC as a complementary tool to support the analysis of identified intact proteins in top-down, middle-down, and/or targeted selected reaction monitoring (SRM)-based proteomic experiments. Figure Intact protein LC retention time prediction assists protein identification in top- and middle-down proteomics