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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/123456789/10468
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dc.contributor.authorSakarellos-Daitsiotis, M.en
dc.contributor.authorTsikaris, V.en
dc.contributor.authorSakarellos, C.en
dc.contributor.authorVlachoyiannopoulos, P. G.en
dc.contributor.authorTzioufas, A. G.en
dc.contributor.authorMoutsopoulos, H. H.en
dc.date.accessioned2015-11-24T16:56:38Z-
dc.date.available2015-11-24T16:56:38Z-
dc.identifier.issn0264-410X-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/10468-
dc.rightsDefault Licence-
dc.subjectpeptide carriersen
dc.subjectcarriers of immunogenic peptidesen
dc.subjectvaccinesen
dc.subjectsynthesis of carriersen
dc.subjectpeptide conformationen
dc.subjecth-1-nmr spectroscopyen
dc.subjectimmunoassaysen
dc.subjectimmune responseen
dc.subjectautoimmune diseasesen
dc.subjectt-cellen
dc.subjectsynthetic peptidesen
dc.subjectrepetitive epitopeen
dc.subjectsm autoantigenen
dc.subjectspecificityen
dc.subjectautoantibodiesen
dc.subjectantibodiesen
dc.subjectdesignen
dc.subjectvaccinesen
dc.subjectla/ssben
dc.titleA new helicoid-type sequential oligopeptide carrier (SOCn) for developing potent antigens and immunogensen
heal.typejournalArticle-
heal.type.enJournal articleen
heal.type.elΆρθρο Περιοδικούel
heal.identifier.secondary<Go to ISI>://000083201100014-
heal.identifier.secondaryhttp://ac.els-cdn.com/S0264410X99002017/1-s2.0-S0264410X99002017-main.pdf?_tid=9cfa76c76dba9c8d973c38b849498192&acdnat=1333038811_a6ece7df0dfbf28551b4ea75a3443ed9-
heal.languageen-
heal.accesscampus-
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείαςel
heal.publicationDate1999-
heal.abstractA new class of sequential oligopeptide carriers (SOCn) for anchoring antigenic/immunogenic peptides has been constructed. The carrier, formed by the repetitive Lys-Aib-Gly moiety, is designed to display a predetermined 3D structure, so that the attached peptides would obtain a defined spatial orientation. Conformational analysis showed that SOCn, adopt a distorted 3(10)-helical structure, while the coupled peptides preserve their original 'active' structure. Coupling to the carrier may also result to the enhancement of one conformer of the anchored peptide. Tt is concluded that the structure of SOCn offers an optimal presentation of the attached peptides, so that potent antigens or immunogens are generated. (C) 1999 Elsevier Science Ltd. All rights reserved.en
heal.publisherElsevieren
heal.journalNameVaccineen
heal.journalTypepeer reviewed-
heal.fullTextAvailabilityTRUE-
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