A cyclic angiotensin antagonist: [1,8-cysteine)angiotensin II

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Abstract
[Cys(S-acetamidomethyl)1,8]angiotensin II has been synthesized by the solid-phase method and purified by carboxymethylcellulose chromatography and reversed-phase HPLC. Treatment of this peptide with iodine gave the cyclic octapeptide [Cys1,8]angiotensin II, which was isolated by Sephadex G-25 chromatography and reversed-phase HPLC. Comparison of the circular dichroism spectra of the open-chain and cyclic peptides, respectively, demonstrated the existence of a disulfide bond with right-handed chirality in the cyclic peptide. In the isolated rat uterus assay, the open-chain peptide was found to be a potent antagonist of angiotensin II, having approximately 10% of the activity of [Sar1, Ile8]angiotensin II, and the cyclic peptide had about 10% of the antagonist potency of its open-chain synthetic precursor.

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