Influence of sequential oligopeptide carriers on the bioactive structure of conjugated epitopes: Comparative study of the conformation of a Herpes simplex virus glycoprotein gD-1 epitope in the free and conjugated form, and protein "built-in" crystal structure

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dc.contributor.authorKrikorian, D.en
dc.contributor.authorStavrakoudis, A.en
dc.contributor.authorBiris, N.en
dc.contributor.authorSakarellos, C.en
dc.contributor.authorAndreu, D.en
dc.contributor.authorde Oliveira, E.en
dc.contributor.authorMezo, G.en
dc.contributor.authorMajer, Z.en
dc.contributor.authorHudecz, F.en
dc.contributor.authorWelling-Wester, S.en
dc.contributor.authorCung, M. T.en
dc.contributor.authorTsikaris, V.en
dc.date.accessioned2015-11-24T16:39:53Z
dc.date.available2015-11-24T16:39:53Z
dc.identifier.issn0006-3525-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/8203
dc.rightsDefault Licence-
dc.subjectconformation of conjugated epitope peptidesen
dc.subjectglycoprotein d-1 epitopeen
dc.subjectsequential oligopeptide carriersen
dc.subjectsequential oligopeptide carriersen
dc.subjecttetratuftsin carrieren
dc.subjectsynthetic carriersen
dc.subjectcarrier-conjugated epitopesen
dc.subjecttorsion angle dynamicsen
dc.subjectsecondary structureen
dc.subjectsm autoantigenen
dc.subjectt-cellen
dc.subjectbranched polypeptidesen
dc.subjectantibody recognitionen
dc.subjectrepetitive epitopeen
dc.subjectantigenic peptidesen
dc.subjectchemical-shiftsen
dc.subjectdesignen
dc.titleInfluence of sequential oligopeptide carriers on the bioactive structure of conjugated epitopes: Comparative study of the conformation of a Herpes simplex virus glycoprotein gD-1 epitope in the free and conjugated form, and protein "built-in" crystal structureen
heal.abstractSynthetic carriers play an important role in immunogen presentation, due to their ability of inducing improved and specific responses to conjugated epitopes. Their influence on the bio- active conformation of the epitope though admittedly crucial for the relevant in vitro and in vivo applications. is difficult to evaluate, given the usual lack of information on the complex conformational features determined by the nature of the carrier and the mode of ligation. Using the Herpes simplex virus glycoprotein D-1 epitope (Leu(9)-Lys-Nle-Ala-A.vp-Pi-o-Asn-Ai-g-Phe-Ai-,g-Gly-Lys-Asp-Lea(22) ) as a model, we have performed a detailed conformational analysis on the free epitope peptide in solution and on three constructs in which the epitope was conjugated to sequential oligopeptide carriers [Ac-[Lys-Aib-GlY](4)-OH (SOC(4))} (through either a thioether or an anfide bond; Ac: acetyl) and polytuftsin oligomers [H-[Thr-Lys-Pro-Lys-GlY](4)-NH(2) (T20)}, (through a thioether bond). The analysis qf the epitope conformation in the parent protein, in carrier-conjugated and free form, suggests that the beta-turn structure of the -Asp(13)-Pro-Asn-Arg(16) segment is highly conserved and independent of the epitope form. However, small conformational variations were observed at the C-terminal part of the epitope, depending on the nature of the carrier. (c) 2006 Wiley Periodicals.en
heal.accesscampus-
heal.fullTextAvailabilityTRUE-
heal.identifier.primaryDoi 10.1002/Bip.20486-
heal.identifier.secondary<Go to ISI>://000238142200003-
heal.identifier.secondaryhttp://onlinelibrary.wiley.com/store/10.1002/bip.20486/asset/20486_ftp.pdf?v=1&t=h0f8ow41&s=6ae4eded0a790d470f89b79cd6a12101e3863082-
heal.journalNameBiopolymersen
heal.journalTypepeer reviewed-
heal.languageen-
heal.publicationDate2006-
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείαςel
heal.typejournalArticle-
heal.type.elΆρθρο Περιοδικούel
heal.type.enJournal articleen

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