| Title | Cyclic thrombin receptor derived peptide analogues | |
| Authors | D. Panagiotopoulos1, J.M. Matsoukas1, M. Keramida1, S. Deraos1, H.L.S. Maia2, R. Yamdagni3, Q. Wu3, P. Redstone4, G.J. Moore4, A.A. Laniyonu4, M. Saifeddine4 and M.D. Hollenberg4
1. Department of Chemistry, University of Patras, 26110 Patras, Greece 2. Department of Chemistry, University of Minho, Guaitar, P-4700 Braga, Portugal 3. Department of Chemistry, University of Calgary, T2N 1N4 Calgary, Alberta, Canada 4. Pharmacology & Therapeutics, University of Calgary, T2N 4N1 Calgary, Alberta, Canada |
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| Citation | Panagiotopoulos, D., Matsoukas, J.M., Keramida, M., Deraos, S., Maia, H.L.S., et al.: Cyclic thrombin receptor derived peptide analogues, Epitheorese Klin. Farmakol. Farmakokinet. 9(2-3): 63-65 (1995) | |
| Publication Date | 1995 | |
| Full Text Language | English | |
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| Keywords | Conformational analysis; NMR spectroscopy; SFLLR, peptide analogues | |
| Other Terms | review article | |
| Summary | Cyclic analogues of the active Thrombin Receptor Peptide SFLLR (TRP42-46) have been prepared by the solid phase method purified by reverse-phase HPLC and bioassayed in the gastric and aortic smooth muscle. Cyclization was achieved by forming on amide-linkage between the -NH2 and -COOH groups of the two Leu residues located at the N and C terminal positions of the protected linear precursor Leu-Arg-X-Phe-Leu (X=Gly, Acp, εLys). The pre-cyclic peptides have been synthesized using the acid sensitive 2-chlorotrityl chloride resin as solid support and cyclization was achieved using diisopropylethylamine (DIPEA) and benzotriazol-1-yl-oxy-tris-(dimethylamino)phosphonium hexafluorophosphate (BOP) as coupling reagent. Deprotection with 60% trifluoroacetic acid (TFA) afforded the three cyclic TRP 42-46 analogues C-FLLRG, C-FLLRAcp, C-FLLRKε and their identity, after HPLC was confirmed by FABMS and NMR methods. The synthesized cyclic analogues were found to be potent in the guinea pig gastric longitudinal smooth muscle (LM) but not in rat aortic (RA) rings preparation. Nuclear Overhauser Effect (NOE) spectroscopy of the most potent cyclic analogue C-FLLRKε in DMSO-d6 has also indicated proximity of the Phe/Arg side chains. These data support the recent findings which illustrate that the intrinsic biological activity of the thrombin receptor derived peptides resides in the pentapeptide SFLLR, TRP42-46 and that the phenylalanine and arginine residues at positions 43 and 46 play key roles in the activity of this pentapeptide in smooth muscle systems. | |
| References | 1. Vu, T.K., Hung, D.T., Wheaton, V.I., Coughlin, S.R.: Cell 64: 1057 (1991)
2. Yang, S.G., Laniyonu, A.A., Saifeddine, M., Moore, G.J., Hollenberg, M.D.: Life Sci. 51:1325 (1992) 3. Hollenberg, M.D., Yang, S.G., Laniyonou, A.A., Moore, G.J., Saifeddine, M.: MoL Pharmacol. 42. 186 (1992) 4. Matsoukas, J.M., Hondrelis, J., Agelis, G., Barlos, K., Gatos, D., Ganter, R.C., Moore, D, Moore, G. J.: J. Med. Chem. 37: 2958 (1994) 5. Barlos, K., Gatos, D., Hondrelis, J., Matsoukas, J., Moore, G.J., Schafer, W., Sotiriou, P.: Liebigs Ann. Chem.: 951-955 (1989) |
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Online ISSN 1011-6575
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