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Thrombin inhibitory activity of some polyphenolic compounds

dc.contributor.authorBijak, M.
dc.contributor.authorZiewiecki, R.
dc.contributor.authorSaluk-Bijak, Joanna
dc.contributor.authorPonczek, Michał
dc.contributor.authorPawlaczyk, I.
dc.contributor.authorKrotkiewski, H.
dc.contributor.authorWachowicz, B.
dc.contributor.authorNowak, P.
dc.date.accessioned2016-05-14T14:15:38Z
dc.date.available2016-05-14T14:15:38Z
dc.date.issued2014
dc.identifier.issn1054-2523
dc.identifier.urihttp://hdl.handle.net/11089/18051
dc.description.abstractThrombin, 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.pl_PL
dc.description.sponsorshipThis work was supported by Grant 545/485 and Grant 506/810 from the University of Lodz.pl_PL
dc.language.isoenpl_PL
dc.publisherSpringer USpl_PL
dc.relation.ispartofseriesMedicinal Chemistry Research;5
dc.rightsUznanie autorstwa 3.0 Polska*
dc.rights.urihttp://creativecommons.org/licenses/by/3.0/pl/*
dc.subjectThrombinpl_PL
dc.subjectPolyphenolic compoundspl_PL
dc.subjectFlavonoidspl_PL
dc.subjectProteolytic activitypl_PL
dc.subjectInhibitionpl_PL
dc.titleThrombin inhibitory activity of some polyphenolic compoundspl_PL
dc.typeArticlepl_PL
dc.page.number2324-2337pl_PL
dc.contributor.authorAffiliationUniversity of Lodz, Faculty of Biology and Environmental Protectionpl_PL
dc.contributor.authorAffiliationWroclaw University of Technology, Faculty of Chemistrypl_PL
dc.contributor.authorAffiliationPolish Academy of Sciences, Institute of Immunology and Experimental Therapypl_PL
dc.identifier.eissn1554-8120
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dc.contributor.authorEmailmbijak@biol.uni.lodz.plpl_PL
dc.identifier.doi10.1007/s00044-013-0829-4
dc.relation.volume23pl_PL


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