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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/123456789/8288
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dc.contributor.authorStavrakoudis, A.en
dc.contributor.authorBizos, G.en
dc.contributor.authorEleftheriadis, D.en
dc.contributor.authorKouki, A.en
dc.contributor.authorPanou-Pomonis, E.en
dc.contributor.authorSakarellos-Daitsiotis, M.en
dc.contributor.authorSakarellos, C.en
dc.contributor.authorTsoukatos, D.en
dc.contributor.authorTsikaris, V.en
dc.date.accessioned2015-11-24T16:40:31Z-
dc.date.available2015-11-24T16:40:31Z-
dc.identifier.issn0006-3525-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/8288-
dc.rightsDefault Licence-
dc.subjectcyclic non-rgd containing analoguesen
dc.subjectcystine non-rgd analoguesen
dc.subjectplatelet aggregation inhibitorsen
dc.subjectcyclization on solid supporten
dc.subjectdisulfide bond formationen
dc.subjectarg-gly-aspen
dc.subjectfibrinogen receptor antagonisten
dc.subjectalpha(v)beta(3) antagonistsen
dc.subjectintegrin alpha(iib)beta(3)en
dc.subjectsecondary structureen
dc.subjecthighly potenten
dc.subjectrecognitionen
dc.subjectproteinen
dc.subjectsequenceen
dc.subjectprogramen
dc.titleA three-residue cyclic scaffold of non-RGD containing peptide analogues as platelet aggregation inhibitors: Design, synthesis, and structure-function relationshipsen
heal.typejournalArticle-
heal.type.enJournal articleen
heal.type.elΆρθρο Περιοδικούel
heal.identifier.secondary<Go to ISI>://000171763200004-
heal.identifier.secondaryhttp://onlinelibrary.wiley.com/store/10.1002/1097-0282(2000)56:1<20::AID-BIP1039>3.0.CO;2-K/asset/1039_ftp.pdf?v=1&t=h0e0tmg8&s=6b475f42d9c52f1b77128884daa4dd1ec15edc3e-
heal.languageen-
heal.accesscampus-
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείαςel
heal.publicationDate2000-
heal.abstractAntagonists of fibrinogen at the GPIIb/IIIa receptor, which is the most abundant membrane protein on the platelet surface, are tinder active investigation as potential antithrombotics. The critical interaction between GPIIb/IIIa and fibrinogen can be inhibited by either linear or cyclic RGDS-containing peptides, which have been proved as lead compounds in the design of platelet aggregation inhibitors. In this study we present the design and construction of it new class of cyclic (S,S) non-RGD containing peptide sequences, using two Cys cis a structural scaffold for the development of antiaggregatory agents. The (S,S)-CDC- sequence was incorporated as a conformational constraint, in molecules bearing at least one positive charge with the general formula (S,S)XCDCZ, where X = Ac-Arg, Pro-Arg, Pro-Ser-Lys, and Pro-Ser-Arg, and Z = -NH2 and Arg-NH2. Investigation of the structure-function relationships was performed on the basis of (a) the local conformation induced by the (S,S)-CDC motif (b) the distance of the positively (R-C-zeta or K-N-zeta) and negatively (D-C-gamma) charged centers, (c) the presence of a second positive or negative charge on the molecule, and (d) the orientation of the basic and acidic side chains defined by, the pseudo dihedral angle (Pdo), which is formed by, the R-C-zeta, R-C-alpha, D-C-alpha, and D-C-gamma atoms in the case of (S,S)-RCDC and by the K-A K-C-alpha, D-C-alpha, and D-C-gamma atoms in the case of (S,S)-KCDC (C) 2001 John Wiley & Sons, Inc.en
heal.publisherWileyen
heal.journalNameBiopolymersen
heal.journalTypepeer reviewed-
heal.fullTextAvailabilityTRUE-
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