Nmr and Mass Spectroscopic Studies of the Competitive-Angiotensin II Antagonist “Sarmesin” |
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Authors: | John M Matsoukas Graham J Moore |
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Institution: | 1. Department of Chemistry , University of Patras Patras , Greece;2. Department of Medical Biochemistry , University of Calgary , Calgary, Alberta, Canada , T2N 4N1 |
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Abstract: | Fast atom bombardment mass spectrometry (FAB-MS) and high resolution (400 Mz) proton nuclear magnetic resonance (NMR spectroscopy) on the competitive angiotensin II antagonist, |Sar1, Tyr(Me)4 (ANGII (Sarmesin) and its he-ptapeptide homolog, Tyr(Me)3 |ANGIII, yield spectra which provide confirmation of structure and molecular weight. The characteristics of the spectra are discussed and compared with the spectra of natural ANG II, ANG III and |Sar1|ANG II. The NMR data are suggestive of interactions in angiotensin between: 1) the phenolic hydroxyl group and the imidazole ring, and 2) the N-terminal amino group and the Tyrring. These interactions may be important for the formation of the proposed charge transfer system in angiotensin II involving the phenoxyl and α-carboxylate groups. |
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Keywords: | Angiotensin conformation receptor binding signal recognition and transduction |
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