The position of the LysN(epsilon)H(2)-grafted antigens along the sequential oligopeptide carrier, Ac-(Aib-Lys-Aib-Gly)(n) (SOCn-II), influences the antibody recognition: Application to the Sm main autoimmune epitope
dc.contributor.author | Alexopoulos, C. | en |
dc.contributor.author | Tsikaris, V. | en |
dc.contributor.author | Rizou, C. | en |
dc.contributor.author | Sakarellos-Daitsiotis, M. | en |
dc.contributor.author | Sakarellos, C. | en |
dc.contributor.author | Cung, M. T. | en |
dc.contributor.author | Marraud, M. | en |
dc.contributor.author | Vlachoyiannopoulos, P. G. | en |
dc.contributor.author | Moutsopoulos, H. M. | en |
dc.date.accessioned | 2015-11-24T16:50:59Z | |
dc.date.available | 2015-11-24T16:50:59Z | |
dc.identifier.issn | 0006-3525 | - |
dc.identifier.uri | https://olympias.lib.uoi.gr/jspui/handle/123456789/9669 | |
dc.rights | Default Licence | - |
dc.subject | sequential oligopeptide carrier | en |
dc.subject | antigenic peptides | en |
dc.subject | socn | en |
dc.subject | sm antigen | en |
dc.subject | 3(10)-helix | en |
dc.subject | circular-dichroism spectra | en |
dc.subject | synthetic-peptide | en |
dc.subject | repetitive epitope | en |
dc.subject | alpha-helices | en |
dc.subject | amino-acids | en |
dc.subject | spectroscopy | en |
dc.subject | specificity | en |
dc.subject | secondary | en |
dc.subject | protein | en |
dc.subject | design | en |
dc.title | The position of the LysN(epsilon)H(2)-grafted antigens along the sequential oligopeptide carrier, Ac-(Aib-Lys-Aib-Gly)(n) (SOCn-II), influences the antibody recognition: Application to the Sm main autoimmune epitope | en |
heal.abstract | A sequential oligopeptide carrier of antigenic peptides is presented, incorporating two Aib residues in each repetitive moiety: Ac-(Aib-Lys-Aib-Gly)(n), (SOCn-II; n = 2-4). The conformational study, by H-1-nmr, CD, and Fourier transform ir spectroscopy; indicated that the SOCn-II carrier displays a pronounced 3(10)-helix, compared to the Ac-(Lys-Aib-Gly)(n) (SOCn-I) carrier of the same approximately backbone length, previously reported One of the dominant autoimmune epitopes of the Sm and U1RNP cellular components, the PPGMRPP sequence, was coupled to the Lys-(NH2)-H-epsilon groups of the SOCn-II carrier and used as antigenic substrate for detecting anti-Sm/ U1RNP autoantibodies in ELISA assays. Anti-Sm antibodies are highly specific for systemic lupus erythematosus, while anti-U1RNP are specific for mixed connective tissue disease. The anti-(PPGMRPP)(5)-SOCn-II ELISA was compared with the anti-(PPGMRPP)(n)-SOCn-I ELISA, provided that both antigenic substrates possess the same amount of the epitope replicates. The significance of the lysine positions along the oligopeptide backbone of the carrier for a favorable antibody recognition of the anchored antigens is also examined. (C) 2000 John Wiley & Sons, Inc. Biopoly 54: 1-10, 2000. | en |
heal.access | campus | - |
heal.fullTextAvailability | TRUE | - |
heal.identifier.secondary | <Go to ISI>://000087289500001 | - |
heal.identifier.secondary | http://onlinelibrary.wiley.com/store/10.1002/(SICI)1097-0282(200007)54:1<1::AID-BIP10>3.0.CO;2-7/asset/10_ftp.pdf?v=1&t=h0e0ip2g&s=5cb0295ab7c8a3bd303ef0df6736f300becfb4e2 | - |
heal.journalName | Biopolymers | en |
heal.journalType | peer reviewed | - |
heal.language | en | - |
heal.publicationDate | 2000 | - |
heal.publisher | Wiley | en |
heal.recordProvider | Πανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείας | el |
heal.type | journalArticle | - |
heal.type.el | Άρθρο Περιοδικού | el |
heal.type.en | Journal article | en |
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