| Title | Differences in backbone structure between the super agonist [Sar1] angiotensin II and its type I antagonist sarilesin | |
| Authors | J.M. Matsoukas1, K. Alexopoulos1, T. Tselios1, P. Roumelioti1, R. Yamdagni2, Q. Wu2, T. Mavromoustakos3, E. Kalatzis3, E. Siapi3 and G.J. Moore4
1. Department of Chemistry, University of Patras, Patras 26500, Greece 2. Department of Chemistry, University of Calgary, Calgary Alberta, Canada T2N 4N1 3. Institute of Organic and Pharmaceutical Chemistry, National Hellenic Research Foundation, Athens 11635, Greece 4. Department of Pharmacology and Therapeutics, University of Calgary, Calgary Alberta T2N 4N1, Canada |
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| Citation | Matsoukas, J.M., Alexopoulos, K., Tselios, T., Roumelioti, P., Yamdagni, R. et al.: Differences in backbone structure between the super agonist [Sar1] angiotensin II and its type I antagonist sarilesin, Epitheorese Klin. Farmakol. Farmakokinet. 11(2-3): 132-136 (1997) | |
| Publication Date | 1997 | |
| Full Text Language | English | |
| Order – Buy | pharmakonpress[at]pharmakonpress[.]gr | |
| Keywords | [Sar1] Angiotensin II, super agonist, type 1 antagonist, Sarilesin, backbone structure | |
| Other Terms | review article | |
| Summary | Conformational investigation of the backbone structure of the super agonist [Sar¹] Angiotensin II and its type I antagonist Sarilesin by one-dimensional Nuclear Overhauser Effect (NOE) spectroscopy revealed that the Tyr-lle-His bend, a conformational property found in ANG H and [Sar1] ANG H is not present in Sarilesin and type I antagonists. In particular, very strong enhancements (17-22%) of Tyr Cα proton resonance in [Sar¹] ANG II upon irradiation of the His Cα proton resonance and vice versa, revealed that Tyr-lle-His bend is a predominant feature of the conformation of the agonist in the receptor simulating environments provided by DMSO-d6 and DMSO-d6/D20 (9/1). In contrast, saturation of the His CQ proton NOE enhancements, illustrating the absence of a Tyr-lle-His bend in the antagonist peptide. The present findings reveal that the phenylalanine ring in the c-terminal residue of the super agonist [Sar¹] ANG II appears to have an essential role in generating the biologically active conformation of the hormone in which the Tyr-lle-His bend is an important structural element allowing a ring duster which triggers activity. Furthermore these data provide for the first time an important backbone conformational difference between [Sar1] ANG II and Sarilesin even they differ chemically, only in the C-terminal residue which is aromatic for the agonist and aliphatic for the antagonist peptides. | |
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Online ISSN 1011-6575
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