Investigation of Interactions between Thrombin and Ten Phenolic Compounds by Affinity Capillary Electrophoresis and Molecular Docking
Thrombin plays a vital role in blood coagulation, which is a key process involved in thrombosis by promoting platelet aggregation and converting fibrinogen to form the fibrin clot. In the receptor concept, drugs produce their therapeutic effects via interactions with the targets. Therefore, investig...
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| Format: | Article |
| Language: | English |
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Wiley
2018-01-01
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| Series: | Journal of Analytical Methods in Chemistry |
| Online Access: | http://dx.doi.org/10.1155/2018/4707609 |
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| author | Qiao-Qiao Li Yu-Xiu Yang Jing-Wen Qv Guang Hu Yuan-Jia Hu Zhi-Ning Xia Feng-Qing Yang |
| author_facet | Qiao-Qiao Li Yu-Xiu Yang Jing-Wen Qv Guang Hu Yuan-Jia Hu Zhi-Ning Xia Feng-Qing Yang |
| author_sort | Qiao-Qiao Li |
| collection | DOAJ |
| description | Thrombin plays a vital role in blood coagulation, which is a key process involved in thrombosis by promoting platelet aggregation and converting fibrinogen to form the fibrin clot. In the receptor concept, drugs produce their therapeutic effects via interactions with the targets. Therefore, investigation of interaction between thrombin and small molecules is important to find out the potential thrombin inhibitor. In this study, affinity capillary electrophoresis (ACE) and in silico molecular docking methods were developed to study the interaction between thrombin and ten phenolic compounds (p-hydroxybenzoic acid, protocatechuic acid, vanillic acid, gallic acid, catechin, epicatechin, dihydroquercetin, naringenin, apigenin, and baicalein). The ACE results showed that gallic acids and six flavonoid compounds had relative strong interactions with thrombin. In addition, the docking results indicated that all of optimal conformations of the six flavonoid compounds were positioned into the thrombin activity centre and had interaction with the HIS57 or SER195 which was the key residue to bind thrombin inhibitors such as argatroban. Herein, these six flavonoid compounds might have the potential of thrombin inhibition activity. In addition, the developed method in this study can be further applied to study the interactions of other molecules with thrombin. |
| format | Article |
| id | doaj-art-becff11da8194a4e84ccdb0f72465681 |
| institution | Kabale University |
| issn | 2090-8865 2090-8873 |
| language | English |
| publishDate | 2018-01-01 |
| publisher | Wiley |
| record_format | Article |
| series | Journal of Analytical Methods in Chemistry |
| spelling | doaj-art-becff11da8194a4e84ccdb0f724656812025-02-03T01:07:09ZengWileyJournal of Analytical Methods in Chemistry2090-88652090-88732018-01-01201810.1155/2018/47076094707609Investigation of Interactions between Thrombin and Ten Phenolic Compounds by Affinity Capillary Electrophoresis and Molecular DockingQiao-Qiao Li0Yu-Xiu Yang1Jing-Wen Qv2Guang Hu3Yuan-Jia Hu4Zhi-Ning Xia5Feng-Qing Yang6School of Chemistry and Chemical Engineering, Chongqing University, Chongqing 401331, ChinaSchool of Chemistry and Chemical Engineering, Chongqing University, Chongqing 401331, ChinaState Key Laboratory of Quality Research in Chinese Medicine, Institute of Chinese Medical Sciences, University of Macau, Macau, ChinaSchool of Pharmacy and Bioengineering, Chongqing University of Technology, Chongqing 400054, ChinaState Key Laboratory of Quality Research in Chinese Medicine, Institute of Chinese Medical Sciences, University of Macau, Macau, ChinaSchool of Chemistry and Chemical Engineering, Chongqing University, Chongqing 401331, ChinaSchool of Chemistry and Chemical Engineering, Chongqing University, Chongqing 401331, ChinaThrombin plays a vital role in blood coagulation, which is a key process involved in thrombosis by promoting platelet aggregation and converting fibrinogen to form the fibrin clot. In the receptor concept, drugs produce their therapeutic effects via interactions with the targets. Therefore, investigation of interaction between thrombin and small molecules is important to find out the potential thrombin inhibitor. In this study, affinity capillary electrophoresis (ACE) and in silico molecular docking methods were developed to study the interaction between thrombin and ten phenolic compounds (p-hydroxybenzoic acid, protocatechuic acid, vanillic acid, gallic acid, catechin, epicatechin, dihydroquercetin, naringenin, apigenin, and baicalein). The ACE results showed that gallic acids and six flavonoid compounds had relative strong interactions with thrombin. In addition, the docking results indicated that all of optimal conformations of the six flavonoid compounds were positioned into the thrombin activity centre and had interaction with the HIS57 or SER195 which was the key residue to bind thrombin inhibitors such as argatroban. Herein, these six flavonoid compounds might have the potential of thrombin inhibition activity. In addition, the developed method in this study can be further applied to study the interactions of other molecules with thrombin.http://dx.doi.org/10.1155/2018/4707609 |
| spellingShingle | Qiao-Qiao Li Yu-Xiu Yang Jing-Wen Qv Guang Hu Yuan-Jia Hu Zhi-Ning Xia Feng-Qing Yang Investigation of Interactions between Thrombin and Ten Phenolic Compounds by Affinity Capillary Electrophoresis and Molecular Docking Journal of Analytical Methods in Chemistry |
| title | Investigation of Interactions between Thrombin and Ten Phenolic Compounds by Affinity Capillary Electrophoresis and Molecular Docking |
| title_full | Investigation of Interactions between Thrombin and Ten Phenolic Compounds by Affinity Capillary Electrophoresis and Molecular Docking |
| title_fullStr | Investigation of Interactions between Thrombin and Ten Phenolic Compounds by Affinity Capillary Electrophoresis and Molecular Docking |
| title_full_unstemmed | Investigation of Interactions between Thrombin and Ten Phenolic Compounds by Affinity Capillary Electrophoresis and Molecular Docking |
| title_short | Investigation of Interactions between Thrombin and Ten Phenolic Compounds by Affinity Capillary Electrophoresis and Molecular Docking |
| title_sort | investigation of interactions between thrombin and ten phenolic compounds by affinity capillary electrophoresis and molecular docking |
| url | http://dx.doi.org/10.1155/2018/4707609 |
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