Cyclic Lactam Analogs Containing the Main Immunogenic Region of Torpedo Acetylcholine-Receptor

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dc.contributor.authorDetsikas, E.en
dc.contributor.authorTsikaris, V.en
dc.contributor.authorSakarellos-Daitsiotis, M.en
dc.contributor.authorSakarellos, C.en
dc.contributor.authorCung, M. T.en
dc.contributor.authorMarraud, M.en
dc.contributor.authorVatzaki, E.en
dc.contributor.authorTzartos, S. J.en
dc.date.accessioned2015-11-24T16:55:11Z
dc.date.available2015-11-24T16:55:11Z
dc.identifier.issn1040-5704-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/10269
dc.rightsDefault Licence-
dc.subjectmonoclonal-antibodiesen
dc.subjectactivity profilesen
dc.subjectalpha-subuniten
dc.subjectside-chainen
dc.subjectpeptidesen
dc.subjectconformationsen
dc.subjectresiduesen
dc.subjectcyclizationsen
dc.subjectlocalizationen
dc.subjectproteinsen
dc.titleCyclic Lactam Analogs Containing the Main Immunogenic Region of Torpedo Acetylcholine-Receptoren
heal.abstractThe majority of autoantibodies against the nicotinic acetylcholine receptor (AChR) bind to an extracellular region of the AChR's alpha-subunit, named main immunogenic region (MIR), with the sequence W67-N-P-A-D-Y-G-G-I-K76 for the Torpedo californica electric organ. We report on the synthesis and the biological and H-1-NMR studies of two cyclic MIR compounds-namely, [D71,K76]-MIR-NH2 and Ac-[Orn68,D71,A76]-MIR-NH2. The relatively small chemical shift differences between [D71,K76]-MIR-NH2 and the biologically active [A76]-analogue suggest that both MIR derivatives possess similar conformations. Thus, the observed limited anti-MIR MAb binding capacity of [D71,K76]-MIR-NH2 is attributed to the D71,K76 side-chain blockage, through lactam. Formation of the Orn68,D71 cycle in the Ac-[Orn68,D71,A76]-MIR-NH2 preserves, unchanged, the low antigenicity of the linear Ac-[Orn68,A76]-MIR-NH2, thus confirming the key role of position 68. The low temperature coefficient value of A70-NH and the observed NOE effect between P69-C(delta)H2 and A70-NH in Ac-[Orn68, D71,A76]-MIR-NH2 argue in favor of a type I beta-turn in the Trp67-Orn-P-A70 sequence. However, the N-terminus beta-folding and the Orn68,D71 cycle appear ineffective for optimal antibody molecular recognition.en
heal.accesscampus-
heal.fullTextAvailabilityTRUE-
heal.identifier.secondary<Go to ISI>://A1993KL67100004-
heal.journalNamePeptide Researchen
heal.journalTypepeer reviewed-
heal.languageen-
heal.publicationDate1993-
heal.publisherEaton Publishing Co.en
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείαςel
heal.typejournalArticle-
heal.type.elΆρθρο Περιοδικούel
heal.type.enJournal articleen

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