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  5. Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά). ΧΗΜ
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Please use this identifier to cite or link to this item: https://olympias.lib.uoi.gr/jspui/handle/123456789/9313
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dc.contributor.authorStanica, R. M.en
dc.contributor.authorBenaki, D.en
dc.contributor.authorRodis, F. I.en
dc.contributor.authorMikros, E.en
dc.contributor.authorTsoukatos, D.en
dc.contributor.authorTselepis, A.en
dc.contributor.authorTsikaris, V.en
dc.date.accessioned2015-11-24T16:48:23Z-
dc.date.available2015-11-24T16:48:23Z-
dc.identifier.issn1075-2617-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/9313-
dc.rightsDefault Licence-
dc.subjectalpha(iib) binding sitesen
dc.subjectarginine interactionsen
dc.subjectaspartic acid interactionsen
dc.subjectfibrinogen inhibitorsen
dc.subjectintegrin alpha(iib)beta(3)en
dc.subjectnmr of peptidesen
dc.subjectrgd conformationen
dc.subjectsarsen
dc.subjectfibrinogen bindingen
dc.subjectintegrin alpha(iib)beta(3)en
dc.subjectthrombastheniaen
dc.subjectactivationen
dc.subjectarginineen
dc.subjectconformationsen
dc.subjectguanidiniumen
dc.subjectgpiib/iiiaen
dc.subjectreceptoren
dc.subjecth-1-nmren
dc.titleStructure-activity relationships of alpha(IIb) 313-320 derived peptide inhibitors of human platelet aggregationen
heal.typejournalArticle-
heal.type.enJournal articleen
heal.type.elΆρθρο Περιοδικούel
heal.identifier.primaryDoi 10.1002/Psc.1060-
heal.identifier.secondary<Go to ISI>://000260926800005-
heal.identifier.secondaryhttp://onlinelibrary.wiley.com/store/10.1002/psc.1060/asset/1060_ftp.pdf?v=1&t=h0f8951x&s=ec8ac62921f6af8dc5837b92e460abac77a7bdb9-
heal.languageen-
heal.accesscampus-
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείαςel
heal.publicationDate2008-
heal.abstractThe alpha(IIb)beta(3) receptor, which is the most abundant receptor on the surface of platelets, can interact with a variety of adhesive proteins including fibrinogen, fibronectin and the von Willebrand factor. Fibrinogen binding on alpha(IIb)beta(3) is an event essential for platelet aggregation and thrombus formation. Mapping of the fibrinogen-binding domains on alpha(IIb) subunit suggested the sequence 313-332 as a possible binding site. This region was restricted to sequence alpha(IIb) 313-320 (Y(313)MESRADR(320)) using synthetic octapeptides overlapping by six residues. The YMESRADR octapeptide inhibits ADP-stimulated human platelets aggregation and binds to immobilized fibrinogen. In this study, we used the Ala scanning methodology within the sequence 313-320 aiming to evaluate the contribution of each amino acid in inhibiting platelet aggregation. It was found that the substitution of Y-313, M-314, E-315 or S-316 by A does not affect the activity of the parent, octapeptide. The-RADR-motif seems to be the most essential for the biological activity of the all,, 313-320 site. The conformational analysis of the YAESRADR, YMESAADR and YMESRAAR analogs by using NMR spectroscopy and distance geometry calculations revealed significant differences in their conformational states. in DMSO-d(6). Copyright (C) 2008 European Peptide Society and John Wiley & Sons, Ltd.en
heal.publisherEuropean Peptide Society and John Wiley & Sons, Ltd.en
heal.journalNameJournal of Peptide Scienceen
heal.journalTypepeer reviewed-
heal.fullTextAvailabilityTRUE-
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