2-Dimensional H-1-Nmr Study of Antigen-Antibody Interactions - Binding of Synthetic Decapeptides to an Antiacetylcholine Receptor Monoclonal-Antibody

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dc.contributor.authorCung, M. T.en
dc.contributor.authorDemange, P.en
dc.contributor.authorMarraud, M.en
dc.contributor.authorTsikaris, V.en
dc.contributor.authorSakarellos, C.en
dc.contributor.authorPapadouli, I.en
dc.contributor.authorKokla, A.en
dc.contributor.authorTzartos, S. J.en
dc.date.accessioned2015-11-24T16:41:27Z
dc.date.available2015-11-24T16:41:27Z
dc.identifier.issn0006-3525-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/8421
dc.rightsDefault Licence-
dc.subjectmain immunogenic regionen
dc.subjecttwo-dimensional h-1-nmren
dc.subjectmyasthenia-gravisen
dc.subjectalpha-subuniten
dc.subjectlocalizationen
dc.subjectdegradationen
dc.subjectresiduesen
dc.subjectmuscleen
dc.subjectmoleculeen
dc.subjectpeptidesen
dc.title2-Dimensional H-1-Nmr Study of Antigen-Antibody Interactions - Binding of Synthetic Decapeptides to an Antiacetylcholine Receptor Monoclonal-Antibodyen
heal.abstractTwo-dimensional NMR experiments [correlated spectroscopy (COSY) and two-dimensional transferred nuclear Overhauser enhancement spectroscopy (TR-NOESY)] have been applied to study the interactions of a monoclonal antibody (mAb) directed to the main immunogenic region (MIR) of the acetylcholine receptor (AChR), and four synthetic decapeptides from the MIR. The decapeptides were the Torpedo AChR alpha-67-76 fragment (W67-N68-P69-A70-D71-Y72-G73-G74-I75-K76) and its three [A69], [A73], and [A76] analogues. The results led to the following conclusions: (1) the magnitude of the TR-NOE cross peaks does not depend only on the structuration of the peptide in the bound state, but also on restrictions of the mobility, i.e., on the correlation time tau-c, which can be different for every residue; (2) the binding capacity of the synthetic peptides to mAbs measured by radioimmunoassay is directly correlated to the NOE magnitude; and (3) the combined interpretation of the COSY and TR-NOESY experiments gives a qualitative information about the nature and the overall conformation of the sequence which is in contact with the mAb binding site.en
heal.accesscampus-
heal.fullTextAvailabilityTRUE-
heal.identifier.secondary<Go to ISI>://A1991FT39400022-
heal.identifier.secondaryhttp://onlinelibrary.wiley.com/store/10.1002/bip.360310622/asset/360310622_ftp.pdf?v=1&t=h0f8n0ap&s=45b20a047554bc3c69df51af12a52766523747d7-
heal.journalNameBiopolymersen
heal.journalTypepeer reviewed-
heal.languageen-
heal.publicationDate1991-
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείαςel
heal.typejournalArticle-
heal.type.elΆρθρο Περιοδικούel
heal.type.enJournal articleen

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