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DC Field | Value | Language |
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dc.contributor.author | Tsikaris, V. | en |
dc.contributor.author | Sakarellos, C. | en |
dc.contributor.author | Sakarellos-Daitsiotis, M. | en |
dc.contributor.author | Orlewski, P. | en |
dc.contributor.author | Marraud, M. | en |
dc.contributor.author | Cung, M. T. | en |
dc.contributor.author | Vatzaki, E. | en |
dc.contributor.author | Tzartos, S. | en |
dc.date.accessioned | 2015-11-24T16:54:47Z | - |
dc.date.available | 2015-11-24T16:54:47Z | - |
dc.identifier.issn | 0141-8130 | - |
dc.identifier.uri | https://olympias.lib.uoi.gr/jspui/handle/123456789/10198 | - |
dc.rights | Default Licence | - |
dc.subject | antigenic peptide carriers | en |
dc.subject | peptide conformation | en |
dc.subject | nicotinic acetylcholine receptor | en |
dc.subject | h-1 nmr spectroscopy | en |
dc.subject | nuclear-magnetic-resonance | en |
dc.subject | molecular-dynamics | en |
dc.subject | synthetic-peptide | en |
dc.subject | mouth-disease | en |
dc.subject | residues | en |
dc.subject | protein | en |
dc.subject | vaccine | en |
dc.subject | design | en |
dc.subject | localization | en |
dc.subject | hepatitis | en |
dc.title | Construction 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 region | en |
heal.type | journalArticle | - |
heal.type.en | Journal article | en |
heal.type.el | Άρθρο Περιοδικού | el |
heal.identifier.secondary | <Go to ISI>://A1996VP48000007 | - |
heal.identifier.secondary | http://ac.els-cdn.com/0141813096011282/1-s2.0-0141813096011282-main.pdf?_tid=8c88b4585007c3311fcc4fbc5b27467a&acdnat=1333038911_bcb7335f7a64e2745657c105558c4637 | - |
heal.language | en | - |
heal.access | campus | - |
heal.recordProvider | Πανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείας | el |
heal.publicationDate | 1996 | - |
heal.abstract | A 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.publisher | Elsevier | en |
heal.journalName | Int J Biol Macromol | en |
heal.journalType | peer reviewed | - |
heal.fullTextAvailability | TRUE | - |
Appears in Collections: | Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά). ΧΗΜ |
Files in This Item:
File | Description | Size | Format | |
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Tsikaris-1996-Construction and app.pdf | 775.42 kB | Adobe PDF | View/Open Request a copy |
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