1. Repository of OAI
  2. ΑΠΟΘΕΤΗΡΙΟ "ΟΛΥΜΠΙΑΣ"
  3. Σχολή Θετικών Επιστημών
  4. Τμήμα Χημείας
  5. Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά). ΧΗΜ
Ελληνικά   English  
Please use this identifier to cite or link to this item: https://olympias.lib.uoi.gr/jspui/handle/123456789/9413
Full metadata record
DC FieldValueLanguage
dc.contributor.authorMezo, G.en
dc.contributor.authorde Oliveira, E.en
dc.contributor.authorKrikorian, D.en
dc.contributor.authorFeijlbrief, M.en
dc.contributor.authorJakab, A.en
dc.contributor.authorTsikaris, V.en
dc.contributor.authorSakarellos, C.en
dc.contributor.authorWelling-Wester, S.en
dc.contributor.authorAndreu, D.en
dc.contributor.authorHudecz, F.en
dc.date.accessioned2015-11-24T16:49:01Z-
dc.date.available2015-11-24T16:49:01Z-
dc.identifier.issn1043-1802-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/9413-
dc.rightsDefault Licence-
dc.subjectsolid-phase synthesisen
dc.subjectbranched polypeptidesen
dc.subjectchemoselective ligationen
dc.subjectmonoclonal-antibodiesen
dc.subjectpeptide vaccinesen
dc.subjectcarrier designen
dc.subjectlinear-epitopeen
dc.subjectside-chainsen
dc.subjectcolor testen
dc.subjectproteinen
dc.titleSynthesis and comparison of antibody recognition of conjugates containing herpes simplex virus type 1 glycoprotein D epitope VIIen
heal.typejournalArticle-
heal.type.enJournal articleen
heal.type.elΆρθρο Περιοδικούel
heal.identifier.primaryDoi 10.1021/Bc0341122-
heal.identifier.secondary<Go to ISI>://000186725700026-
heal.identifier.secondaryhttp://pubs.acs.org/doi/abs/10.1021/bc0341122-
heal.languageen-
heal.accesscampus-
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείαςel
heal.publicationDate2003-
heal.abstractSynthetic oligopeptides comprising linear or continuous topographic B-cell epitope sequences of proteins might be considered as specific and small size antigens. It has been demonstrated that the strength and specificity of antibody binding could be altered by conjugation to macromolecules or by modification in the flanking regions. However, no systematic studies have been reported to describe the effect of different carrier macromolecules in epitope conjugates. To this end, the influence of carrier structure and topology on antibody recognition of attached epitope has been studied by comparing the antibody binding properties of a new set of conjugates with tetratuftsin analogue (H-[Thr-Lys-Pro-Lys-Gly](4)-NH(2), T20) sequential oligopeptide carrier (SOC(n)), branched chain polypeptide, poly[Lys(Ser(i)-DL-Ala(m))] (SAK), multiple antigenic peptide (MAP), and keyhole limpet hemocyanine (KLH). In these novel constructs, peptide (9)LKNleADPNRFRGKDL(22) ([Nle(11)]-9-22) representing an immunodominant B cell epitope of herpes simplex virus type 1 glycoprotein D (HSV-1 gD) was conjugated to polypeptides through a thioether or amide bond. Here we report on the preparation of sequential and polymeric polypeptides possessing chloroacetyl groups in multiple copies at the alpha- and/or is an element of-amino group of the polypeptides and its use for the conjugation of epitope peptides possessing Cys at C-terminal position. We have performed binding studies (direct and competitive ELISA) with monoclonal antibody (Mab) A16, recognizing the HSV gD-related epitope, [Nle(11)]-9-22, and conjugates containing identical and uniformly oriented epitope peptide in multiple copies attached to five different macromolecules as carrier. Data suggest that the chemical nature of the carrier and the degree of substitution have marked influence on the strength of antibody binding.en
heal.journalNameBioconjugate Chemistryen
heal.journalTypepeer reviewed-
heal.fullTextAvailabilityTRUE-
Appears in Collections:Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά). ΧΗΜ

Show simple item record
Files in This Item:
There are no files associated with this item.
Show simple item record  


This item is licensed under a Creative Commons License Creative Commons