Exploring the interaction of calycosin with cyclin D1 protein as a regulator of cell cycle progression in lung cancer cells
Cyclin D1 has been shown to play a pivotal role in the proliferation of lung cancer cells through regulation of cell cycle progression. Therefore, targeting this protein can be used as a potential strategy in lung cancer treatment. Calycosin has been reported to show potential anticancer effects, ho...
| Main Authors: | , , , , |
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| Format: | Article |
| Language: | English |
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Elsevier
2022-05-01
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| Series: | Arabian Journal of Chemistry |
| Subjects: | |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S1878535222000387 |
| _version_ | 1819023652400660480 |
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| author | Tianci Han Liang Zhang Wei Tong Jian Zhao Wei Wang |
| author_facet | Tianci Han Liang Zhang Wei Tong Jian Zhao Wei Wang |
| author_sort | Tianci Han |
| collection | DOAJ |
| description | Cyclin D1 has been shown to play a pivotal role in the proliferation of lung cancer cells through regulation of cell cycle progression. Therefore, targeting this protein can be used as a potential strategy in lung cancer treatment. Calycosin has been reported to show potential anticancer effects, however, its possible anticancer mechanisms remain unclear. Therefore, in this study we aimed to explore the interaction of cyclin D1 and calycosin to determine the binding properties and probable structural changes of cyclin D1. We carried out in-depth experimental and computational binding assays of calycosin with cyclin D1 under simulated physiological environment, using intrinsic, extrinsic, synchronous fluorescence, circular dichroism, and differential scanning calorimetry (DSC) analysis. The results showed a spontaneous static mechanism driven from hydrogen bonding and van der Waals forces between hydrophilic residues of cyclin D1 with hydroxyl groups of calycosin. We determined that calycosin led to secondary and tertiary structural changes of cyclin D1 through exposure of hydrophobic residues. Also, it was determined that calycosin resulted in an apparent decrease in the heat capacity changes (ΔCp) and midpoint of unfolding transition (Tm) values of cyclin D1. Cellular studies also indicated that calycosin caused the inhibition of lung cancer cell proliferation through cell cycle arrest at G1 phase, which may be due to denaturation of cyclin D1, although it needs further investigation in the future studies. In general, this study may provide useful preliminary data about the development of calycosin-based anticancer platforms. |
| first_indexed | 2024-12-21T04:42:18Z |
| format | Article |
| id | doaj.art-ff6c78441a5642a9aeb92d357d7bf440 |
| institution | Directory Open Access Journal |
| issn | 1878-5352 |
| language | English |
| last_indexed | 2024-12-21T04:42:18Z |
| publishDate | 2022-05-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Arabian Journal of Chemistry |
| spelling | doaj.art-ff6c78441a5642a9aeb92d357d7bf4402022-12-21T19:15:39ZengElsevierArabian Journal of Chemistry1878-53522022-05-01155103722Exploring the interaction of calycosin with cyclin D1 protein as a regulator of cell cycle progression in lung cancer cellsTianci Han0Liang Zhang1Wei Tong2Jian Zhao3Wei Wang4Department of Thoracic Surgery, Cancer Hospital of China Medical University, No. 44 Xiaoheyan Road, Dadong District, Shenyang 110042, Liaoning Province, PR China; Department of Thoracic Surgery, Liaoning Cancer Hospital & Institute, No. 44 Xiaoheyan Road, Dadong District, Shenyang 110042, Liaoning Province, PR ChinaDepartment of Thoracic Surgery, Cancer Hospital of China Medical University, No. 44 Xiaoheyan Road, Dadong District, Shenyang 110042, Liaoning Province, PR China; Department of Thoracic Surgery, Liaoning Cancer Hospital & Institute, No. 44 Xiaoheyan Road, Dadong District, Shenyang 110042, Liaoning Province, PR ChinaDepartment of Thoracic Surgery, Cancer Hospital of China Medical University, No. 44 Xiaoheyan Road, Dadong District, Shenyang 110042, Liaoning Province, PR China; Department of Thoracic Surgery, Liaoning Cancer Hospital & Institute, No. 44 Xiaoheyan Road, Dadong District, Shenyang 110042, Liaoning Province, PR ChinaDepartment of Thoracic Surgery, Cancer Hospital of China Medical University, No. 44 Xiaoheyan Road, Dadong District, Shenyang 110042, Liaoning Province, PR China; Department of Thoracic Surgery, Liaoning Cancer Hospital & Institute, No. 44 Xiaoheyan Road, Dadong District, Shenyang 110042, Liaoning Province, PR ChinaCorresponding author at: No. 44 Xiaoheyan Road, Dadong District, Shenyang 110042, Liaoning Province, PR China.; Department of Thoracic Surgery, Cancer Hospital of China Medical University, No. 44 Xiaoheyan Road, Dadong District, Shenyang 110042, Liaoning Province, PR China; Department of Thoracic Surgery, Liaoning Cancer Hospital & Institute, No. 44 Xiaoheyan Road, Dadong District, Shenyang 110042, Liaoning Province, PR ChinaCyclin D1 has been shown to play a pivotal role in the proliferation of lung cancer cells through regulation of cell cycle progression. Therefore, targeting this protein can be used as a potential strategy in lung cancer treatment. Calycosin has been reported to show potential anticancer effects, however, its possible anticancer mechanisms remain unclear. Therefore, in this study we aimed to explore the interaction of cyclin D1 and calycosin to determine the binding properties and probable structural changes of cyclin D1. We carried out in-depth experimental and computational binding assays of calycosin with cyclin D1 under simulated physiological environment, using intrinsic, extrinsic, synchronous fluorescence, circular dichroism, and differential scanning calorimetry (DSC) analysis. The results showed a spontaneous static mechanism driven from hydrogen bonding and van der Waals forces between hydrophilic residues of cyclin D1 with hydroxyl groups of calycosin. We determined that calycosin led to secondary and tertiary structural changes of cyclin D1 through exposure of hydrophobic residues. Also, it was determined that calycosin resulted in an apparent decrease in the heat capacity changes (ΔCp) and midpoint of unfolding transition (Tm) values of cyclin D1. Cellular studies also indicated that calycosin caused the inhibition of lung cancer cell proliferation through cell cycle arrest at G1 phase, which may be due to denaturation of cyclin D1, although it needs further investigation in the future studies. In general, this study may provide useful preliminary data about the development of calycosin-based anticancer platforms.http://www.sciencedirect.com/science/article/pii/S1878535222000387Cyclin D1CalycosinInteractionSpectroscopyLung cancer |
| spellingShingle | Tianci Han Liang Zhang Wei Tong Jian Zhao Wei Wang Exploring the interaction of calycosin with cyclin D1 protein as a regulator of cell cycle progression in lung cancer cells Arabian Journal of Chemistry Cyclin D1 Calycosin Interaction Spectroscopy Lung cancer |
| title | Exploring the interaction of calycosin with cyclin D1 protein as a regulator of cell cycle progression in lung cancer cells |
| title_full | Exploring the interaction of calycosin with cyclin D1 protein as a regulator of cell cycle progression in lung cancer cells |
| title_fullStr | Exploring the interaction of calycosin with cyclin D1 protein as a regulator of cell cycle progression in lung cancer cells |
| title_full_unstemmed | Exploring the interaction of calycosin with cyclin D1 protein as a regulator of cell cycle progression in lung cancer cells |
| title_short | Exploring the interaction of calycosin with cyclin D1 protein as a regulator of cell cycle progression in lung cancer cells |
| title_sort | exploring the interaction of calycosin with cyclin d1 protein as a regulator of cell cycle progression in lung cancer cells |
| topic | Cyclin D1 Calycosin Interaction Spectroscopy Lung cancer |
| url | http://www.sciencedirect.com/science/article/pii/S1878535222000387 |
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