| Autor: |
Cung, M. T., Demange, P., Marraud, M., Tsikaris, V., Sakarellos, C., Papadouli, I., Kokla, A., Tzartos, S. J. |
| Jazyk: |
angličtina |
| Rok vydání: |
1991 |
| Předmět: |
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| Popis: |
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. Biopolymers |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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