The NMR studies of CMP inhibition of polysialylation
The overexpression of polysialic acid (polySia) on neural cell adhesion molecules (NCAM) promotes hypersialylation, and thus benefits cancer cell migration and invasion. It has been proposed that the binding between the polysialyltransferase domain (PSTD) and CMP-Sia needs to be inhibited in order t...
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| Format: | Article |
| Language: | English |
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Taylor & Francis Group
2023-12-01
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| Series: | Journal of Enzyme Inhibition and Medicinal Chemistry |
| Subjects: | |
| Online Access: | https://www.tandfonline.com/doi/10.1080/14756366.2023.2248411 |
| _version_ | 1827123329501233152 |
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| author | Bo Lu Si-Ming Liao Xue-Hui Liu Shi-Jie Liang Jun Huang Mei Lin Li Meng Qing-Yan Wang Ri-Bo Huang Guo-Ping Zhou |
| author_facet | Bo Lu Si-Ming Liao Xue-Hui Liu Shi-Jie Liang Jun Huang Mei Lin Li Meng Qing-Yan Wang Ri-Bo Huang Guo-Ping Zhou |
| author_sort | Bo Lu |
| collection | DOAJ |
| description | The overexpression of polysialic acid (polySia) on neural cell adhesion molecules (NCAM) promotes hypersialylation, and thus benefits cancer cell migration and invasion. It has been proposed that the binding between the polysialyltransferase domain (PSTD) and CMP-Sia needs to be inhibited in order to block the effects of hypersialylation. In this study, CMP was confirmed to be a competitive inhibitor of polysialyltransferases (polySTs) in the presence of CMP-Sia and triSia (oligosialic acid trimer) based on the interactional features between molecules. The further NMR analysis suggested that polysialylation could be partially inhibited when CMP-Sia and polySia co-exist in solution. In addition, an unexpecting finding is that CMP-Sia plays a role in reducing the gathering extent of polySia chains on the PSTD, and may benefit for the inhibition of polysialylation. The findings in this study may provide new insight into the optimal design of the drug and inhibitor for cancer treatment. |
| first_indexed | 2024-03-09T02:02:39Z |
| format | Article |
| id | doaj.art-3ee323e26107490d828325cb76b0b536 |
| institution | Directory Open Access Journal |
| issn | 1475-6366 1475-6374 |
| language | English |
| last_indexed | 2025-03-20T14:23:12Z |
| publishDate | 2023-12-01 |
| publisher | Taylor & Francis Group |
| record_format | Article |
| series | Journal of Enzyme Inhibition and Medicinal Chemistry |
| spelling | doaj.art-3ee323e26107490d828325cb76b0b5362024-09-09T17:23:19ZengTaylor & Francis GroupJournal of Enzyme Inhibition and Medicinal Chemistry1475-63661475-63742023-12-0138110.1080/14756366.2023.2248411The NMR studies of CMP inhibition of polysialylationBo Lu0Si-Ming Liao1Xue-Hui Liu2Shi-Jie Liang3Jun Huang4Mei Lin5Li Meng6Qing-Yan Wang7Ri-Bo Huang8Guo-Ping Zhou9National Engineering Research Center for Non-food Biorefinery, Guangxi Academy of Sciences, Nanning, Guangxi, ChinaInstitute of Biophysics, Chinese Academy of Sciences, Beijing, ChinaInstitute of Biophysics, Chinese Academy of Sciences, Beijing, ChinaNational Engineering Research Center for Non-food Biorefinery, Guangxi Academy of Sciences, Nanning, Guangxi, ChinaNational Engineering Research Center for Non-food Biorefinery, Guangxi Academy of Sciences, Nanning, Guangxi, ChinaNational Engineering Research Center for Non-food Biorefinery, Guangxi Academy of Sciences, Nanning, Guangxi, ChinaNational Engineering Research Center for Non-food Biorefinery, Guangxi Academy of Sciences, Nanning, Guangxi, ChinaNational Engineering Research Center for Non-food Biorefinery, Guangxi Academy of Sciences, Nanning, Guangxi, ChinaNational Engineering Research Center for Non-food Biorefinery, Guangxi Academy of Sciences, Nanning, Guangxi, ChinaNational Engineering Research Center for Non-food Biorefinery, Guangxi Academy of Sciences, Nanning, Guangxi, ChinaThe overexpression of polysialic acid (polySia) on neural cell adhesion molecules (NCAM) promotes hypersialylation, and thus benefits cancer cell migration and invasion. It has been proposed that the binding between the polysialyltransferase domain (PSTD) and CMP-Sia needs to be inhibited in order to block the effects of hypersialylation. In this study, CMP was confirmed to be a competitive inhibitor of polysialyltransferases (polySTs) in the presence of CMP-Sia and triSia (oligosialic acid trimer) based on the interactional features between molecules. The further NMR analysis suggested that polysialylation could be partially inhibited when CMP-Sia and polySia co-exist in solution. In addition, an unexpecting finding is that CMP-Sia plays a role in reducing the gathering extent of polySia chains on the PSTD, and may benefit for the inhibition of polysialylation. The findings in this study may provide new insight into the optimal design of the drug and inhibitor for cancer treatment.https://www.tandfonline.com/doi/10.1080/14756366.2023.2248411Metastatic spreadpolysialic acidpolysialyltransferasepolysialyltransferase domainchemical shift perturbation |
| spellingShingle | Bo Lu Si-Ming Liao Xue-Hui Liu Shi-Jie Liang Jun Huang Mei Lin Li Meng Qing-Yan Wang Ri-Bo Huang Guo-Ping Zhou The NMR studies of CMP inhibition of polysialylation Journal of Enzyme Inhibition and Medicinal Chemistry Metastatic spread polysialic acid polysialyltransferase polysialyltransferase domain chemical shift perturbation |
| title | The NMR studies of CMP inhibition of polysialylation |
| title_full | The NMR studies of CMP inhibition of polysialylation |
| title_fullStr | The NMR studies of CMP inhibition of polysialylation |
| title_full_unstemmed | The NMR studies of CMP inhibition of polysialylation |
| title_short | The NMR studies of CMP inhibition of polysialylation |
| title_sort | nmr studies of cmp inhibition of polysialylation |
| topic | Metastatic spread polysialic acid polysialyltransferase polysialyltransferase domain chemical shift perturbation |
| url | https://www.tandfonline.com/doi/10.1080/14756366.2023.2248411 |
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