Molecular docking reveals fibrinogen binding sites on SARS-CoV-2 spike protein: A potential mechanism for COVID-19-related coagulation
The Coronavirus Disease (COVID-19) pandemic, caused by Severe Acute Respiratory Syndrome coronavirus-2 (SARS-CoV-2), highlighted significant gaps in our understanding of the virus's molecular structure, its biological properties, and the interactions between viral proteins and host biologic...
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Society of Turaz Bilim
2024-04-01
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| Series: | Medicine Science |
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| Online Access: | https://www.medicinescience.org/?mno=217169 |
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| _version_ | 1825206490861928448 |
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| author | Onur Ozturk Evren Kilinc Batuhan Gorkem Irez Emel Timucin |
| author_facet | Onur Ozturk Evren Kilinc Batuhan Gorkem Irez Emel Timucin |
| author_sort | Onur Ozturk |
| collection | DOAJ |
| description | The Coronavirus Disease (COVID-19) pandemic, caused by Severe Acute Respiratory Syndrome coronavirus-2 (SARS-CoV-2), highlighted significant gaps in our understanding of the virus's molecular structure, its biological properties, and the interactions between viral proteins and host biological systems, which have underscored the critical need for further research in this area. Coagulation disorders, particularly those leading to thromboinflammation, have been linked to severe complications in COVID-19 cases. The occurrence of thromboinflammation has likewise been corroborated in cases of both Severe Acute Respiratory Syndrome (SARS) and Middle East Respiratory Syndrome (MERS). In this study, we investigated the protein-protein interactions between the SARS-CoV-2 spike protein and fibrinogen, a glycoprotein that plays a crucial role in blood coagulation. Molecular docking analysis revealed key interactions between the β and γ subunits of fibrinogen and the spike protein. The findings suggest that these interactions may contribute to the understanding of the coagulation disorders observed in COVID-19 patients. This study provides insights into the molecular mechanisms underlying these disorders and identifies potential targets for the development of therapeutic interventions. [Med-Science 2024; 13(4.000): 803-8] |
| format | Article |
| id | doaj-art-81b6604555414f10bdc766cc66b872fd |
| institution | Kabale University |
| issn | 2147-0634 |
| language | English |
| publishDate | 2024-04-01 |
| publisher | Society of Turaz Bilim |
| record_format | Article |
| series | Medicine Science |
| spelling | doaj-art-81b6604555414f10bdc766cc66b872fd2025-02-07T08:49:23ZengSociety of Turaz BilimMedicine Science2147-06342024-04-01134803810.5455/medscience.2024.08.099217169Molecular docking reveals fibrinogen binding sites on SARS-CoV-2 spike protein: A potential mechanism for COVID-19-related coagulationOnur Ozturk0Evren Kilinc1Batuhan Gorkem Irez2Emel Timucin3Malatya Turgut Ozal University School of Medicine, Department of Biophysics, Malatya, Turkiye University of Health Sciences, Hamidiye Faculty of Medicine, Department of Biophysics, Istanbul, Turkiye Istanbul University, Program of Basic Sciences (TEBIP), Biology Undergraduate, Istanbul, Turkiye Acıbadem University Faculty of Medicine, Department of Basic Medical Sciences, Department of Biostatistics and Medical Informatics, Istanbul, TurkiyeThe Coronavirus Disease (COVID-19) pandemic, caused by Severe Acute Respiratory Syndrome coronavirus-2 (SARS-CoV-2), highlighted significant gaps in our understanding of the virus's molecular structure, its biological properties, and the interactions between viral proteins and host biological systems, which have underscored the critical need for further research in this area. Coagulation disorders, particularly those leading to thromboinflammation, have been linked to severe complications in COVID-19 cases. The occurrence of thromboinflammation has likewise been corroborated in cases of both Severe Acute Respiratory Syndrome (SARS) and Middle East Respiratory Syndrome (MERS). In this study, we investigated the protein-protein interactions between the SARS-CoV-2 spike protein and fibrinogen, a glycoprotein that plays a crucial role in blood coagulation. Molecular docking analysis revealed key interactions between the β and γ subunits of fibrinogen and the spike protein. The findings suggest that these interactions may contribute to the understanding of the coagulation disorders observed in COVID-19 patients. This study provides insights into the molecular mechanisms underlying these disorders and identifies potential targets for the development of therapeutic interventions. [Med-Science 2024; 13(4.000): 803-8]https://www.medicinescience.org/?mno=217169spike proteinfibrinogencoagulationmolecular dockingmolecular structuresevere acute respiratory syndrome coronavirus |
| spellingShingle | Onur Ozturk Evren Kilinc Batuhan Gorkem Irez Emel Timucin Molecular docking reveals fibrinogen binding sites on SARS-CoV-2 spike protein: A potential mechanism for COVID-19-related coagulation Medicine Science spike protein fibrinogen coagulation molecular docking molecular structure severe acute respiratory syndrome coronavirus |
| title | Molecular docking reveals fibrinogen binding sites on SARS-CoV-2 spike protein: A potential mechanism for COVID-19-related coagulation |
| title_full | Molecular docking reveals fibrinogen binding sites on SARS-CoV-2 spike protein: A potential mechanism for COVID-19-related coagulation |
| title_fullStr | Molecular docking reveals fibrinogen binding sites on SARS-CoV-2 spike protein: A potential mechanism for COVID-19-related coagulation |
| title_full_unstemmed | Molecular docking reveals fibrinogen binding sites on SARS-CoV-2 spike protein: A potential mechanism for COVID-19-related coagulation |
| title_short | Molecular docking reveals fibrinogen binding sites on SARS-CoV-2 spike protein: A potential mechanism for COVID-19-related coagulation |
| title_sort | molecular docking reveals fibrinogen binding sites on sars cov 2 spike protein a potential mechanism for covid 19 related coagulation |
| topic | spike protein fibrinogen coagulation molecular docking molecular structure severe acute respiratory syndrome coronavirus |
| url | https://www.medicinescience.org/?mno=217169 |
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