Two-Dimensional 1H-nmr study of antigen–antibody interactions: Binding of synthetic decapeptides to an anti-acetylcholine receptor monoclonal antibody
✍ Scribed by Manh Thong Cung; Pascal Demange; Michel Marraud; Vassilios Tsikaris; Constantinos Sakarellos; Irene Papadouli; Anna Kokla; Socrates J. Tzartos
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1991
- Tongue
- English
- Weight
- 656 KB
- Volume
- 31
- Category
- Article
- ISSN
- 0006-3525
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✦ Synopsis
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 a67-76 fragment ( W 67-N68-P69-A70-D71-Y 72-G73-G74-175-K7fi) and its three [A"], [ A73], and [ A7'] 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 T , , 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.
in One and Two Dimensions, Clarendon Press, Oxford.