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Thrombin inhibitory activity of some polyphenolic compounds
Thrombin, also known as an active plasma coagulation factor II, belongs to the family of serine proteases and plays a crucial role in blood coagulation process. The process of thrombin generation is the central event of the hemostatic process and regulates blood coagulant activity. For this reason,...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Springer US
2013
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3939009/ https://www.ncbi.nlm.nih.gov/pubmed/24610996 http://dx.doi.org/10.1007/s00044-013-0829-4 |
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author | Bijak, M. Ziewiecki, R. Saluk, J. Ponczek, M. Pawlaczyk, I. Krotkiewski, H. Wachowicz, B. Nowak, P. |
author_facet | Bijak, M. Ziewiecki, R. Saluk, J. Ponczek, M. Pawlaczyk, I. Krotkiewski, H. Wachowicz, B. Nowak, P. |
author_sort | Bijak, M. |
collection | PubMed |
description | Thrombin, also known as an active plasma coagulation factor II, belongs to the family of serine proteases and plays a crucial role in blood coagulation process. The process of thrombin generation is the central event of the hemostatic process and regulates blood coagulant activity. For this reason, thrombin inhibition is key to successful novel antithrombotic pharmacotherapy. The aim of our present study was to examine the effects of the well-known polyphenolic compounds on the activity of thrombin, by characterization of its interaction with selected polyphenols using different biochemical methods and biosensor BIAcore analyses. Only six compounds, cyanidin, quercetin, silybin, cyanin, (+)-catechin and (−)-epicatechin, of all examined in this study polyphenols caused the inhibition of thrombin amidolytic activity. But only three of the six compounds (cyanidin, quercetin and silybin) changed thrombin proteolytic activity. BIAcore analyses demonstrated that cyanidin and quercetin caused a strong response in the interaction with immobilized thrombin, while cyanin and (−)-epicatechin induced a low response. Lineweaver–Burk curves show that used polyphenol aglycones act as competitive thrombin inhibitors. Our results suggest that polyphenolic compounds might be potential structural bases and source to find and project nature-based, safe, orally bioavailable direct thrombin inhibitors. |
format | Online Article Text |
id | pubmed-3939009 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | Springer US |
record_format | MEDLINE/PubMed |
spelling | pubmed-39390092014-03-06 Thrombin inhibitory activity of some polyphenolic compounds Bijak, M. Ziewiecki, R. Saluk, J. Ponczek, M. Pawlaczyk, I. Krotkiewski, H. Wachowicz, B. Nowak, P. Med Chem Res Original Research Thrombin, also known as an active plasma coagulation factor II, belongs to the family of serine proteases and plays a crucial role in blood coagulation process. The process of thrombin generation is the central event of the hemostatic process and regulates blood coagulant activity. For this reason, thrombin inhibition is key to successful novel antithrombotic pharmacotherapy. The aim of our present study was to examine the effects of the well-known polyphenolic compounds on the activity of thrombin, by characterization of its interaction with selected polyphenols using different biochemical methods and biosensor BIAcore analyses. Only six compounds, cyanidin, quercetin, silybin, cyanin, (+)-catechin and (−)-epicatechin, of all examined in this study polyphenols caused the inhibition of thrombin amidolytic activity. But only three of the six compounds (cyanidin, quercetin and silybin) changed thrombin proteolytic activity. BIAcore analyses demonstrated that cyanidin and quercetin caused a strong response in the interaction with immobilized thrombin, while cyanin and (−)-epicatechin induced a low response. Lineweaver–Burk curves show that used polyphenol aglycones act as competitive thrombin inhibitors. Our results suggest that polyphenolic compounds might be potential structural bases and source to find and project nature-based, safe, orally bioavailable direct thrombin inhibitors. Springer US 2013-10-16 2014 /pmc/articles/PMC3939009/ /pubmed/24610996 http://dx.doi.org/10.1007/s00044-013-0829-4 Text en © The Author(s) 2013 https://creativecommons.org/licenses/by/2.0/ Open AccessThis article is distributed under the terms of the Creative Commons Attribution License which permits any use, distribution, and reproduction in any medium, provided the original author(s) and the source are credited. |
spellingShingle | Original Research Bijak, M. Ziewiecki, R. Saluk, J. Ponczek, M. Pawlaczyk, I. Krotkiewski, H. Wachowicz, B. Nowak, P. Thrombin inhibitory activity of some polyphenolic compounds |
title | Thrombin inhibitory activity of some polyphenolic compounds |
title_full | Thrombin inhibitory activity of some polyphenolic compounds |
title_fullStr | Thrombin inhibitory activity of some polyphenolic compounds |
title_full_unstemmed | Thrombin inhibitory activity of some polyphenolic compounds |
title_short | Thrombin inhibitory activity of some polyphenolic compounds |
title_sort | thrombin inhibitory activity of some polyphenolic compounds |
topic | Original Research |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3939009/ https://www.ncbi.nlm.nih.gov/pubmed/24610996 http://dx.doi.org/10.1007/s00044-013-0829-4 |
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