Barnase-Barstar Pair: Contemporary Application in Cancer Research and Nanotechnology
Barnase is an extracellular ribonuclease secreted by <i>Bacillus amyloliquefaciens</i> that was originally studied as a small stable enzyme with robust folding. The identification of barnase intracellular inhibitor barstar led to the discovery of an incredibly strong protein-protein inte...
| Main Authors: | , , , , |
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| Format: | Article |
| Language: | English |
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MDPI AG
2021-11-01
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| Series: | Molecules |
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| Online Access: | https://www.mdpi.com/1420-3049/26/22/6785 |
| _version_ | 1797509134201913344 |
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| author | Olga Shilova Polina Kotelnikova Galina Proshkina Elena Shramova Sergey Deyev |
| author_facet | Olga Shilova Polina Kotelnikova Galina Proshkina Elena Shramova Sergey Deyev |
| author_sort | Olga Shilova |
| collection | DOAJ |
| description | Barnase is an extracellular ribonuclease secreted by <i>Bacillus amyloliquefaciens</i> that was originally studied as a small stable enzyme with robust folding. The identification of barnase intracellular inhibitor barstar led to the discovery of an incredibly strong protein-protein interaction. Together, barnase and barstar provide a fully genetically encoded toxin-antitoxin pair having an extremely low dissociation constant. Moreover, compared to other dimerization systems, the barnase-barstar module provides the exact one-to-one ratio of the complex components and possesses high stability of each component in a complex and high solubility in aqueous solutions without self-aggregation. The unique properties of barnase and barstar allow the application of this pair for the engineering of different variants of targeted anticancer compounds and cytotoxic supramolecular complexes. Using barnase in suicide gene therapy has also found its niche in anticancer therapy. The application of barnase and barstar in contemporary experimental cancer therapy is reflected in the review. |
| first_indexed | 2024-03-10T05:14:29Z |
| format | Article |
| id | doaj.art-1e22c4ccfb084fbea663ee1b8ad81500 |
| institution | Directory Open Access Journal |
| issn | 1420-3049 |
| language | English |
| last_indexed | 2024-03-10T05:14:29Z |
| publishDate | 2021-11-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Molecules |
| spelling | doaj.art-1e22c4ccfb084fbea663ee1b8ad815002023-11-23T00:33:42ZengMDPI AGMolecules1420-30492021-11-012622678510.3390/molecules26226785Barnase-Barstar Pair: Contemporary Application in Cancer Research and NanotechnologyOlga Shilova0Polina Kotelnikova1Galina Proshkina2Elena Shramova3Sergey Deyev4Shemyakin & Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, 117997 Moscow, RussiaShemyakin & Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, 117997 Moscow, RussiaShemyakin & Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, 117997 Moscow, RussiaShemyakin & Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, 117997 Moscow, RussiaShemyakin & Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, 117997 Moscow, RussiaBarnase is an extracellular ribonuclease secreted by <i>Bacillus amyloliquefaciens</i> that was originally studied as a small stable enzyme with robust folding. The identification of barnase intracellular inhibitor barstar led to the discovery of an incredibly strong protein-protein interaction. Together, barnase and barstar provide a fully genetically encoded toxin-antitoxin pair having an extremely low dissociation constant. Moreover, compared to other dimerization systems, the barnase-barstar module provides the exact one-to-one ratio of the complex components and possesses high stability of each component in a complex and high solubility in aqueous solutions without self-aggregation. The unique properties of barnase and barstar allow the application of this pair for the engineering of different variants of targeted anticancer compounds and cytotoxic supramolecular complexes. Using barnase in suicide gene therapy has also found its niche in anticancer therapy. The application of barnase and barstar in contemporary experimental cancer therapy is reflected in the review.https://www.mdpi.com/1420-3049/26/22/6785barnasebarstarcancer therapynanoparticles |
| spellingShingle | Olga Shilova Polina Kotelnikova Galina Proshkina Elena Shramova Sergey Deyev Barnase-Barstar Pair: Contemporary Application in Cancer Research and Nanotechnology Molecules barnase barstar cancer therapy nanoparticles |
| title | Barnase-Barstar Pair: Contemporary Application in Cancer Research and Nanotechnology |
| title_full | Barnase-Barstar Pair: Contemporary Application in Cancer Research and Nanotechnology |
| title_fullStr | Barnase-Barstar Pair: Contemporary Application in Cancer Research and Nanotechnology |
| title_full_unstemmed | Barnase-Barstar Pair: Contemporary Application in Cancer Research and Nanotechnology |
| title_short | Barnase-Barstar Pair: Contemporary Application in Cancer Research and Nanotechnology |
| title_sort | barnase barstar pair contemporary application in cancer research and nanotechnology |
| topic | barnase barstar cancer therapy nanoparticles |
| url | https://www.mdpi.com/1420-3049/26/22/6785 |
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