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|
|Link:||<Go to ISI>://A1993LJ21500013|
|Appears in Collections:||Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά)|
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