A diepitopic sequential oligopeptide carrier (SOCn) as mimic of the Sm autoantigen: Synthesis, conformation and biological assays

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dc.contributor.authorAlexopoulos, C.en
dc.contributor.authorTsikaris, V.en
dc.contributor.authorRizou, C.en
dc.contributor.authorPanou-Pomonis, E.en
dc.contributor.authorSakarellos-Daitsiotis, M.en
dc.contributor.authorSakarellos, C.en
dc.contributor.authorVlachoyiannopoulos, P. G.en
dc.contributor.authorMoutsopoulos, H. M.en
dc.date.accessioned2015-11-24T16:54:38Z
dc.date.available2015-11-24T16:54:38Z
dc.identifier.issn1075-2617-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/10179
dc.rightsDefault Licence-
dc.subjectcarrier of the sm epitopesen
dc.subjectdiepitopic sequential oligopeptide carrieren
dc.subjectnmr study of socnen
dc.subjectsequential oligopeptide carriers (soc)(n)en
dc.subjectsm autoantigenen
dc.subjectsm epitopes grafted to socnen
dc.subjectsm mimicen
dc.subjectglycopeptide dendrimersen
dc.subjectrepetitive epitopeen
dc.subjectantigenic peptidesen
dc.subjectresidual wateren
dc.subjectautoantibodiesen
dc.subjectprotectionen
dc.subjectallylen
dc.titleA diepitopic sequential oligopeptide carrier (SOCn) as mimic of the Sm autoantigen: Synthesis, conformation and biological assaysen
heal.abstractAnti-Sm (Sm: U1-U6 RNA-protein complex) antibodies are usually considered highly specific for systemic lupus erythematosus (SLE), while anti-U1RNP (U1RNP: U1RNA-protein complex) are thought of as diagnostic criteria for the mixed connective tissue disease (MCTD). However, both antibody specificities coexist in SLE and MCTD, in varying percentages. Although the anti-Sm/anti-U1RNP immunological cross-reactivity has been initially attributed to a common motif, PPXY(Z)PP (where X, Y, Z are various amino acids), found in the Sm, U1-A and U1-C autoantigens, it appears that the conformational features of the Sm epitopes also play an important role in the immunoreactivity. The PPGMRPP and PPGIRGP main epitopes of the Sm antigen were coupled in duplicate to the tetrameric Ac-(Lys-Aib-Gly)(4)-OH, SOC4, carrier to form the [(PPGMRPP)(2), (PPGIRGP)(2)]-SOC4 construct as a mimic of the native Sm. It was found that: (i) the 3(10) helical structure of SOC, allows the epitopes to adopt an exposed orientation, similar to their free forms, that facilitates their recognition from the anti-Sm antibodies, and (ii) the U1-RNP cross-reactivity is minimized. Copyright (C) 2001 European Peptide Society and John Wiley & Sons, Ltd.en
heal.accesscampus-
heal.fullTextAvailabilityTRUE-
heal.identifier.secondary<Go to ISI>://000167522100005-
heal.identifier.secondaryhttp://onlinelibrary.wiley.com/store/10.1002/psc.302/asset/302_ftp.pdf?v=1&t=h0e0j7j6&s=7f7b00c74a7993fb8568de3020ff82af17d27409-
heal.journalNameJournal of Peptide Scienceen
heal.journalTypepeer reviewed-
heal.languageen-
heal.publicationDate2001-
heal.publisherWileyen
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείαςel
heal.typejournalArticle-
heal.type.elΆρθρο Περιοδικούel
heal.type.enJournal articleen

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