Protein Interactome Profiling of Stable Molecular Complexes in Biomaterial Lysate
Most proteins function as part of various complexes, forming via stable and dynamic protein–protein interactions (PPIs). The profiling of PPIs expands the fundamental knowledge about the structures, functions, and regulation patterns of protein complexes and intracellular molecular machineries. Prot...
| Main Authors: | , , , , , , |
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| Format: | Article |
| Language: | English |
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MDPI AG
2022-12-01
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| Series: | International Journal of Molecular Sciences |
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| Online Access: | https://www.mdpi.com/1422-0067/23/24/15697 |
| _version_ | 1797457242934476800 |
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| author | Yuri Mezentsev Pavel Ershov Evgeniy Yablokov Leonid Kaluzhskiy Konstantin Kupriyanov Oksana Gnedenko Alexis Ivanov |
| author_facet | Yuri Mezentsev Pavel Ershov Evgeniy Yablokov Leonid Kaluzhskiy Konstantin Kupriyanov Oksana Gnedenko Alexis Ivanov |
| author_sort | Yuri Mezentsev |
| collection | DOAJ |
| description | Most proteins function as part of various complexes, forming via stable and dynamic protein–protein interactions (PPIs). The profiling of PPIs expands the fundamental knowledge about the structures, functions, and regulation patterns of protein complexes and intracellular molecular machineries. Protein interactomics aims at solving three main tasks: (1) identification of protein partners and parts of complex intracellular structures; (2) analysis of PPIs parameters (affinity, molecular-recognition specificity, kinetic rate constants, and thermodynamic-parameters determination); (3) the study of the functional role of novel PPIs. The purpose of this work is to update the current state and prospects of multi-omics approaches to profiling of proteins involved in the formation of stable complexes. Methodological paradigm includes a development of protein-extraction and -separation techniques from tissues or cellular lysates and subsequent identification of proteins using mass-spectrometry analysis. In addition, some aspects of authors’ experimental platforms, based on high-performance size-exclusion chromatography, procedures of molecular fishing, and protein identification, as well as the possibilities of interactomic taxonomy of each protein, are discussed. |
| first_indexed | 2024-03-09T16:19:24Z |
| format | Article |
| id | doaj.art-13e5971f0022480c838480daa02de10c |
| institution | Directory Open Access Journal |
| issn | 1661-6596 1422-0067 |
| language | English |
| last_indexed | 2024-03-09T16:19:24Z |
| publishDate | 2022-12-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | International Journal of Molecular Sciences |
| spelling | doaj.art-13e5971f0022480c838480daa02de10c2023-11-24T15:26:15ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672022-12-0123241569710.3390/ijms232415697Protein Interactome Profiling of Stable Molecular Complexes in Biomaterial LysateYuri Mezentsev0Pavel Ershov1Evgeniy Yablokov2Leonid Kaluzhskiy3Konstantin Kupriyanov4Oksana Gnedenko5Alexis Ivanov6Institute of Biomedical Chemistry (IBMC), 119121 Moscow, RussiaInstitute of Biomedical Chemistry (IBMC), 119121 Moscow, RussiaInstitute of Biomedical Chemistry (IBMC), 119121 Moscow, RussiaInstitute of Biomedical Chemistry (IBMC), 119121 Moscow, RussiaInstitute of Biomedical Chemistry (IBMC), 119121 Moscow, RussiaInstitute of Biomedical Chemistry (IBMC), 119121 Moscow, RussiaInstitute of Biomedical Chemistry (IBMC), 119121 Moscow, RussiaMost proteins function as part of various complexes, forming via stable and dynamic protein–protein interactions (PPIs). The profiling of PPIs expands the fundamental knowledge about the structures, functions, and regulation patterns of protein complexes and intracellular molecular machineries. Protein interactomics aims at solving three main tasks: (1) identification of protein partners and parts of complex intracellular structures; (2) analysis of PPIs parameters (affinity, molecular-recognition specificity, kinetic rate constants, and thermodynamic-parameters determination); (3) the study of the functional role of novel PPIs. The purpose of this work is to update the current state and prospects of multi-omics approaches to profiling of proteins involved in the formation of stable complexes. Methodological paradigm includes a development of protein-extraction and -separation techniques from tissues or cellular lysates and subsequent identification of proteins using mass-spectrometry analysis. In addition, some aspects of authors’ experimental platforms, based on high-performance size-exclusion chromatography, procedures of molecular fishing, and protein identification, as well as the possibilities of interactomic taxonomy of each protein, are discussed.https://www.mdpi.com/1422-0067/23/24/15697interactomicsprotein–protein interactionsmass-spectrometric identificationsize-exclusion chromatographyinteractome taxonomy of proteinsstable protein complexes |
| spellingShingle | Yuri Mezentsev Pavel Ershov Evgeniy Yablokov Leonid Kaluzhskiy Konstantin Kupriyanov Oksana Gnedenko Alexis Ivanov Protein Interactome Profiling of Stable Molecular Complexes in Biomaterial Lysate International Journal of Molecular Sciences interactomics protein–protein interactions mass-spectrometric identification size-exclusion chromatography interactome taxonomy of proteins stable protein complexes |
| title | Protein Interactome Profiling of Stable Molecular Complexes in Biomaterial Lysate |
| title_full | Protein Interactome Profiling of Stable Molecular Complexes in Biomaterial Lysate |
| title_fullStr | Protein Interactome Profiling of Stable Molecular Complexes in Biomaterial Lysate |
| title_full_unstemmed | Protein Interactome Profiling of Stable Molecular Complexes in Biomaterial Lysate |
| title_short | Protein Interactome Profiling of Stable Molecular Complexes in Biomaterial Lysate |
| title_sort | protein interactome profiling of stable molecular complexes in biomaterial lysate |
| topic | interactomics protein–protein interactions mass-spectrometric identification size-exclusion chromatography interactome taxonomy of proteins stable protein complexes |
| url | https://www.mdpi.com/1422-0067/23/24/15697 |
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