Design, synthesis, and conformational study of biologically active photolabeled analogues of the main immunogenic region of the acetylcholine receptor

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dc.contributor.authorTheodorou, V.en
dc.contributor.authorTsikaris, V.en
dc.contributor.authorSakarellos-Daitsiotis, M.en
dc.contributor.authorAvramopoulou, V.en
dc.contributor.authorKostelidou, K.en
dc.contributor.authorTzartos, S. J.en
dc.contributor.authorSakarellos, C.en
dc.date.accessioned2015-11-24T16:55:28Z
dc.date.available2015-11-24T16:55:28Z
dc.identifier.issn0006-3525-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/10313
dc.rightsDefault Licence-
dc.subjectacetylcholine receptoren
dc.subjectmyasthenia gravisen
dc.subjectmain immunogenic regionen
dc.subjectanti-mir antibodiesen
dc.subjectcomplementarity determining regionsen
dc.subjectphotolabelingen
dc.subjectphotoaffinityen
dc.subjectbenzoylphenylalanineen
dc.subjectmir structureen
dc.subjectmonoclonal-antibodiesen
dc.subjectparathyroid-hormoneen
dc.subjectbimolecular interactionen
dc.subjectmolecular recognitionen
dc.subjectsubstrate recognitionen
dc.subjectalpha-67-76 fragmenten
dc.subjectprotein-receptoren
dc.subjectbinding domainen
dc.subjectcross-linkingen
dc.subjectalpha-subuniten
dc.titleDesign, synthesis, and conformational study of biologically active photolabeled analogues of the main immunogenic region of the acetylcholine receptoren
heal.abstractPhotoaffinity labeling is a powerful tool for the characterization of the molecular basis of ligand binding to acceptor molecules, which provides important insights for mapping the bimolecular interfaces. The autoimmune disease myasthenia gravis is caused by autoantibodies against the acetylcholine receptor (AChR). The majority, of the anti-AChR antibodies bind to the "main immunogenic region" (MIR) of the AChR. To identify, the contact points between the complementarity determining regions of the anti-MIR antibodies that recognize the MIR contact sites of the AChR, we present here three photoreactive dodecapeptide MIR analogues containing the photolabel p-benzoyl-L-phenylalanine (Bpa) moiety, either in position 1 or 11. The structure of the produced 12-mers was analyzed using two-dimensional H-1-NMR spectroscopy, whereas their binding to anti-MIR monoclonal antibodies (mAbs) was determined by immunochemical assays. In all cases the modifications resulted in conservation of the beta -turn conformation of the N-terminus, which has been proved essential for antibody recognition and increased anti-MIR binding relative to the MIR decapeptide. (C) 2001 John Wiley & Sons, Inc.en
heal.accesscampus-
heal.fullTextAvailabilityTRUE-
heal.identifier.secondary<Go to ISI>://000171763200006-
heal.identifier.secondaryhttp://onlinelibrary.wiley.com/store/10.1002/1097-0282(2000)56:1<37::AID-BIP1041>3.0.CO;2-X/asset/1041_ftp.pdf?v=1&t=hn1hi7s1&s=f5b9b726c716f463c7840288216b1a6132cea510-
heal.journalNameBiopolymersen
heal.journalTypepeer reviewed-
heal.languageen-
heal.publicationDate2001-
heal.publisherWiley-Blackwellen
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείαςel
heal.typejournalArticle-
heal.type.elΆρθρο Περιοδικούel
heal.type.enJournal articleen

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