2-Dimensional H-1-Nmr Study of Antigen-Antibody Interactions - Binding of Synthetic Decapeptides to an Antiacetylcholine Receptor Monoclonal-Antibody (Journal article)
Cung, M. T./ Demange, P./ Marraud, M./ Tsikaris, V./ Sakarellos, C./ Papadouli, I./ Kokla, A./ Tzartos, S. J.
Two-dimensional NMR experiments [correlated spectroscopy (COSY) and two-dimensional transferred nuclear Overhauser enhancement spectroscopy (TR-NOESY)] have been applied to study the interactions of a monoclonal antibody (mAb) directed to the main immunogenic region (MIR) of the acetylcholine receptor (AChR), and four synthetic decapeptides from the MIR. The decapeptides were the Torpedo AChR alpha-67-76 fragment (W67-N68-P69-A70-D71-Y72-G73-G74-I75-K76) and its three [A69], [A73], and [A76] analogues. The results led to the following conclusions: (1) the magnitude of the TR-NOE cross peaks does not depend only on the structuration of the peptide in the bound state, but also on restrictions of the mobility, i.e., on the correlation time tau-c, which can be different for every residue; (2) the binding capacity of the synthetic peptides to mAbs measured by radioimmunoassay is directly correlated to the NOE magnitude; and (3) the combined interpretation of the COSY and TR-NOESY experiments gives a qualitative information about the nature and the overall conformation of the sequence which is in contact with the mAb binding site.
|Institution and School/Department of submitter:||Πανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείας|
|Keywords:||main immunogenic region,two-dimensional h-1-nmr,myasthenia-gravis,alpha-subunit,localization,degradation,residues,muscle,molecule,peptides|
|Link:||<Go to ISI>://A1991FT39400022|
|Appears in Collections:||Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά)|
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