Conformational Requirements for Molecular Recognition of Acetylcholine-Receptor Main Immunogenic Region (Mir) Analogs by Monoclonal Anti-Mir Antibody - a 2-Dimensional Nuclear-Magnetic-Resonance and Molecular-Dynamics Approach

Απλή σελίδα τεκμηρίου
dc.contributor.authorTsikaris, V.en
dc.contributor.authorDetsikas, E.en
dc.contributor.authorSakarellosdaitsiotis, M.en
dc.contributor.authorSakarellos, C.en
dc.contributor.authorVatzaki, E.en
dc.contributor.authorTzartos, S. J.en
dc.contributor.authorMarraud, M.en
dc.contributor.authorCung, M. T.en
dc.date.accessioned2015-11-24T16:54:45Z
dc.date.available2015-11-24T16:54:45Z
dc.identifier.issn0006-3525-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/10191
dc.rightsDefault Licence-
dc.subjecttwo-dimensional h-1-nmren
dc.subjectsynthetic peptidesen
dc.subjectmyasthenia-gravisen
dc.subjectalpha-subuniten
dc.subjectresiduesen
dc.subjectlocalizationen
dc.subjectaciden
dc.titleConformational Requirements for Molecular Recognition of Acetylcholine-Receptor Main Immunogenic Region (Mir) Analogs by Monoclonal Anti-Mir Antibody - a 2-Dimensional Nuclear-Magnetic-Resonance and Molecular-Dynamics Approachen
heal.abstractThe conformational properties of two [D-A70, A76] and [Aib70, A76] analogues of the alpha67-76 Torpedo acetylcholine receptor fragment, with low binding capacity for the anti main immunogenic region (MIR) antibodies, were studied in DMSO by two-dimensional nmr techniques and molecular dynamics simulations. The results were compared to the free and bound conformations of the [A76] analogue, which has twice more affinity for the anti-MIR monoclonal antibody 6 (mAb6), than the natural Torpedo sequence. It appeared that a single substitution of the A70, at a crucial position, by the D-A70 or Aib70 ,could modify completely the conformational behavior of the peptide and reduced its recognition by the anti-MIR antibody. The WNPADY rigid structure at the N-terminal part was essential for antibody recognition. The adjacent more flexible C-terminal sequence (GGIK) gives additional stability to the monoclonal antibody-peptide complex probably due to an adequate orientation of the peptide side chains in the complex, by setting them in close contact with the antibody.en
heal.accesscampus-
heal.fullTextAvailabilityTRUE-
heal.identifier.secondary<Go to ISI>://A1993LJ21500013-
heal.identifier.secondaryhttp://onlinelibrary.wiley.com/store/10.1002/bip.360330714/asset/360330714_ftp.pdf?v=1&t=h0e0tsgg&s=7587c8eeafcbe96a8d95e52d84b0a5db7638876f-
heal.journalNameBiopolymersen
heal.journalTypepeer reviewed-
heal.languageen-
heal.publicationDate1993-
heal.publisherWileyen
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείαςel
heal.typejournalArticle-
heal.type.elΆρθρο Περιοδικούel
heal.type.enJournal articleen

Αρχεία

Φάκελος/Πακέτο αδειών

Προβολή: 1 - 1 of 1
Μικρογραφία εικόνας
Ονομα:
license.txt
Μέγεθος:
1.74 KB
Μορφότυπο:
Item-specific license agreed upon to submission
Περιγραφή:
Κατεβάστε

Συλλογές

Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά). ΧΗΜ