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 (Journal article)

Tsikaris, V./ Detsikas, E./ Sakarellosdaitsiotis, M./ Sakarellos, C./ Vatzaki, E./ Tzartos, S. J./ Marraud, M./ Cung, M. T.

The 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.
Institution and School/Department of submitter: Πανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείας
Keywords: two-dimensional h-1-nmr,synthetic peptides,myasthenia-gravis,alpha-subunit,residues,localization,acid
ISSN: 0006-3525
Link: <Go to ISI>://A1993LJ21500013
Publisher: Wiley
Appears in Collections:Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά)

Files in This Item:
File Description SizeFormat 
Tsikaris-1993-Conformational Requi.pdf890.47 kBAdobe PDFView/Open    Request a copy

 Please use this identifier to cite or link to this item:
  This item is a favorite for 0 people.

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.