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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/123456789/10198
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dc.contributor.authorTsikaris, V.en
dc.contributor.authorSakarellos, C.en
dc.contributor.authorSakarellos-Daitsiotis, M.en
dc.contributor.authorOrlewski, P.en
dc.contributor.authorMarraud, M.en
dc.contributor.authorCung, M. T.en
dc.contributor.authorVatzaki, E.en
dc.contributor.authorTzartos, S.en
dc.date.accessioned2015-11-24T16:54:47Z-
dc.date.available2015-11-24T16:54:47Z-
dc.identifier.issn0141-8130-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/10198-
dc.rightsDefault Licence-
dc.subjectantigenic peptide carriersen
dc.subjectpeptide conformationen
dc.subjectnicotinic acetylcholine receptoren
dc.subjecth-1 nmr spectroscopyen
dc.subjectnuclear-magnetic-resonanceen
dc.subjectmolecular-dynamicsen
dc.subjectsynthetic-peptideen
dc.subjectmouth-diseaseen
dc.subjectresiduesen
dc.subjectproteinen
dc.subjectvaccineen
dc.subjectdesignen
dc.subjectlocalizationen
dc.subjecthepatitisen
dc.titleConstruction and application of a new class of sequential oligopeptide carriers (SOCn) for multiple anchoring of antigenic peptides - Application to the acetylcholine receptor (AChR) main immunogenic regionen
heal.typejournalArticle-
heal.type.enJournal articleen
heal.type.elΆρθρο Περιοδικούel
heal.identifier.secondary<Go to ISI>://A1996VP48000007-
heal.identifier.secondaryhttp://ac.els-cdn.com/0141813096011282/1-s2.0-0141813096011282-main.pdf?_tid=8c88b4585007c3311fcc4fbc5b27467a&acdnat=1333038911_bcb7335f7a64e2745657c105558c4637-
heal.languageen-
heal.accesscampus-
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείαςel
heal.publicationDate1996-
heal.abstractA new class of sequential oligopeptide carriers (SOCn), namely (Lys-Aib-Gly)(n) (n=2-7), for anchoring antigenic peptides, is presented. These SOCn have been designed in order to assume a determined structural motif, exhibiting defined spatial orientations of the Lys-(NH2)-H-epsilon anchoring groups. The NMR study showed that SOCn adopt a rigid conformation with some regularity, initiated from the C-terminus of the carrier, while molecular dynamics simulation confirmed the occurrence of a distorted 3(10)-helix. It was also demonstrated, by (1)HNMR, that all the antigenic peptides bound to the SOCn retain their original, folded active, structure and that probably they do not interact to each other. It is concluded that the beneficial structural elements of the SOCn impose a favorable disposition of the anchored peptides so that potent antigens with maximum molecular recognition are generated.en
heal.publisherElsevieren
heal.journalNameInt J Biol Macromolen
heal.journalTypepeer reviewed-
heal.fullTextAvailabilityTRUE-
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