| Title | Conformational properties and biological activity of torpedo acetylcholine MIR-analogues | |
| Authors | M. Sakarellos-Daitsiotis1, V. Tsikaris1, E. Detsikas1, C. Sakarellos1, E. Vatzaki2, S. Tzartos2, M. Marraud3 and M.T. Cung3
1. Department of Chemistry, University of Ioannina, Box 1186, 45110 Ioannina, Greece 2. Department of Biochemistry, Hellenic Pasteur Institute, 127 Vassilissis Sofias Avenue, 11521 Athens, Greece 3. Laboratoire de Chimie-Physique Macromoléculaire, CNRS-URA 494, ENSIC-INPL, 1 rue Grandville, BP 451, 54001 Nancy Cedex France |
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| Citation | Sakarellos-Daitsiotis,M., Tsikaris, V., Detsikas, E., Sakarellos, C., Vatzaki, E. et al.: Conformational properties and biological activity of torpedo acetylcholine MIR-analogues, Epitheorese Klin. Farmakol. Farmakokinet. 9(2-3): 109-111 (1995) | |
| Publication Date | 1995 | |
| Full Text Language | English | |
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| Keywords | Acetylcholine receptor, conformational analysis, NMR, a-subunit. | |
| Other Terms | review article | |
| Summary | In the Myasthenia Gravis disease, most of the antibodies are directed against an extracellular area, called main immunogenic region (MIR), of the α-subunit of the acetylcholine receptor (AChR). The conformation of some decapeptide analogues of the α67-76 MIR fragment of the Torpedo fish and human muscle AChR with different mAb binding potencies was examined in the absence or in the presence of two anti-MIR mAb6 (Torpedo) and mAb (human) by 2D-NMR experiments (COSY and transferred NOESY). More or less intense NOE effects were observed depending to the mAb binding potencies. These effects were quantized and used as distance constraints for the molecular dynamics (MD) calculation (using SYBYL and BIOGROMOS programs). Previous NMR and MD studies evidenced the existence of a β-turn in the N-terminal part of the molecule and some mobility of the C-terminal part for a good recognition by the mAbs. Recent results have shown that the simultaneous substitution of the residues 70 and 76 could modify completely the conformational behaviour of the peptide and induced its recognition either by the mAbs (Torpedo) or by the mAb 198 human MIR antibody. | |
| References | 1. Barkas, T., Gabriel, J.M., Manson, A., Hughes, G.J., Roth, B., Alliod, C., Tzartos, S.J., Bellivet, M.: J. Biol. Chem. 263: 5916 (1988)
2. Papadouli, I., Potamianos, S. Hadjidakis, I., Bairaktari, E., Tsikaris V., Sakarellos, C., Cung, M.T., Marraud, M., Tzartos, J.S.: Biochem. J. 269: 239 (1990) 3. Cung, M.T., Tsikaris, V., Demartge, P., Papadouli, I., Tzartos, J.S., Sakarellos, C., Marraud, M.: Peptide Res. 5: 14 (1992) 4. Wuthrich, Κ.: NMR of Proteins and Nucleic Adds. John Wiley and Sons, New York, 1986 |
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Online ISSN 1011-6575
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| ΕΤΗΣΙΑ ΣΥΝΔΡΟΜΗ 1995 – ANNUAL SUBSCRIPTION 1995 | |
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