1. Repository of OAI
  2. ΑΠΟΘΕΤΗΡΙΟ "ΟΛΥΜΠΙΑΣ"
  3. Σχολή Θετικών Επιστημών
  4. Τμήμα Χημείας
  5. Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά). ΧΗΜ
Ελληνικά   English  
Please use this identifier to cite or link to this item: https://olympias.lib.uoi.gr/jspui/handle/123456789/8102
Full metadata record
DC FieldValueLanguage
dc.contributor.authorKouki, A.en
dc.contributor.authorMitsios, J. V.en
dc.contributor.authorSakarellos-Daitsiotis, M.en
dc.contributor.authorSakarellos, C.en
dc.contributor.authorTselepis, A. D.en
dc.contributor.authorTsikaris, V.en
dc.contributor.authorTsoukatos, D. C.en
dc.date.accessioned2015-11-24T16:38:55Z-
dc.date.available2015-11-24T16:38:55Z-
dc.identifier.issn1538-7933-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/8102-
dc.rightsDefault Licence-
dc.subjectantiaggregatory agentsen
dc.subjectfibrinogen-binding inhibitorsen
dc.subjectintegrin alpha(iib)beta(3) inhibitorsen
dc.subjectplatelet activation inhibitorsen
dc.subjectglycoprotein-iib-iiiaen
dc.subjectiib/iiia antagonistsen
dc.subjectrgd peptidesen
dc.subjectintegrin alpha(iib)beta(3)en
dc.subjectreceptoren
dc.subjectactivationen
dc.subjectadhesionen
dc.subjectargen
dc.subjectalpha(iib)-subuniten
dc.subjectalpha-v-beta-3en
dc.titleHighly constrained cyclic (S,S) -CXaaC- peptides as inhibitors of fibrinogen binding to plateletsen
heal.typejournalArticle-
heal.type.enJournal articleen
heal.type.elΆρθρο Περιοδικούel
heal.identifier.secondary<Go to ISI>://000232443200027-
heal.identifier.secondaryhttp://onlinelibrary.wiley.com/store/10.1111/j.1538-7836.2005.01487.x/asset/j.1538-7836.2005.01487.x.pdf?v=1&t=h0e0mukc&s=bd858378361b7b854624f7bce6ae970e03459e0f-
heal.languageen-
heal.accesscampus-
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείαςel
heal.publicationDate2005-
heal.abstractThe Arg-Gly-Asp RGD motif of adhesive proteins is recognized by the activated platelet integrin alpha(IIb)beta 3. Binding of fibrinogen (Fg) to activated alpha(IIb)beta(3) causes platelet aggregation and thrombus formation. Highly constraint cyclic (S,S) CXaaC- containing peptides incorporating the (S,S) -CDC- and (S,.S) -CRC- motifs were tested for their ability to inhibit platelet aggregation and Fg binding. Our results suggest that the above cyclic scaffolds stabilize a favorable structure for the antiaggregatory activity (IC50-values ranged from 1.7 to 570 pm). The peptides inhibited Fg binding with IC50-values up to 30-fold lower than those determined for the inhibition of the adenosine diphosphate (ADP)-induced platelet aggregation. Importantly, peptides (S,S) PSRCDCR-NH2 (peptide 11) and (S,S) PRCDCK-NH2 (peptide 10) did not inhibit PAC-1 binding to the activated platelets at a concentration in which they completely inhibited Fg binding. Moreover, (S,S) PSRCDCR-NH2 (peptide 11), one of the more active peptides, inhibited ADP-induced P-selectin exposure. By contrast, peptide (S,S) Ac-RWDCRC-NH2, incorporating the inverse (S,S)-DCRC-sequence (peptide 16), failed to inhibit P-selectin exposure whereas at the same concentration, it effectively inhibited PAG I and Fg binding. It is concluded that peptides containing the (S,S) -CDC- as well the (S,S) -CRC- sequences, exhibit a broad range of activities toward platelets, and could be helpful tools for elucidating the structural interaction of Fg with the integrin receptor alpha(IIb)beta(3), in its activated form. Furthermore, the (S,S) RCDC- sequence can be used as a scaffold for developing potent non-RGD-like Fg-binding inhibitors.en
heal.publisherBlackwell Publishingen
heal.journalNameJournal of Thrombosis and Haemostasisen
heal.journalTypepeer reviewed-
heal.fullTextAvailabilityTRUE-
Appears in Collections:Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά). ΧΗΜ

Show simple item record
Files in This Item:
File Description SizeFormat 
Kouki-2005-Highly constrained c.pdf260.28 kBAdobe PDFView/Open    Request a copy
Show simple item record  


This item is licensed under a Creative Commons License Creative Commons