Sequential oligopetide carriers, SOCn, as scaffolds for the reconstitution of antigenic proteins: applications in solid phase immunoassays

dc.contributor.authorSakarellos-Daitsiotis, M.en
dc.contributor.authorAlexopoulos, C.en
dc.contributor.authorSakarellos, C.en
dc.date.accessioned2015-11-24T16:47:01Z
dc.date.available2015-11-24T16:47:01Z
dc.identifier.issn0731-7085-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/9131
dc.rightsDefault Licence-
dc.subjectoligopeptide carriersen
dc.subjectantigenic proteinsen
dc.subjectsolid phase immunoassaysen
dc.subjectmain immunogenic regionen
dc.subjectnicotinic acetylcholine-receptoren
dc.subjectanti-sm antibodiesen
dc.subjectoligopeptide carriersen
dc.subjectglycopeptide dendrimersen
dc.subjectsynthetic peptideen
dc.subjectepitopeen
dc.subjectautoantibodiesen
dc.subjectspecificityen
dc.subjectdesignen
dc.titleSequential oligopetide carriers, SOCn, as scaffolds for the reconstitution of antigenic proteins: applications in solid phase immunoassaysen
heal.abstractA new class of helicoid type sequential oligopeptide carriers (SOC), for anchoring antigenic epitopes, has been modeled from the repetitive Lys-Aib-Gly (SOCn-I) and Aib-Lys-Aib-Gly (SOCn-II) units aiming to the development of scaffolds with predetermined 3D structures. Conformational analysis showed that the SOCn carriers adopt 3(10)-helical structures, while the SOCn-conjugates retain their original active conformations and they interact neither to the carriers nor to each other. It is concluded that the helicoid structure of SOC,, helps the reconstitution and/or mimicking of the native forms of the epitopes so that potent antigens are generated for developing specific, sensitive and reproducible immunoassays. (C) 2003 Elsevier B.V. All rights reserved.en
heal.accesscampus-
heal.fullTextAvailabilityTRUE-
heal.identifier.primaryDoi 10.1016/S0731-7085(03)00561-2-
heal.identifier.secondary<Go to ISI>://000220237600005-
heal.identifier.secondaryhttp://ac.els-cdn.com/S0731708503005612/1-s2.0-S0731708503005612-main.pdf?_tid=ca99cea28e37a9e2463320095358a3e3&acdnat=1333038818_ebd20d32b05b1dd92750c0ef2945b9fe-
heal.journalNameJ Pharm Biomed Analen
heal.journalTypepeer reviewed-
heal.languageen-
heal.publicationDate2004-
heal.publisherElsevieren
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείαςel
heal.typejournalArticle-
heal.type.elΆρθρο Περιοδικούel
heal.type.enJournal articleen

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