Photoaffinity labeling of the angiotensin II receptor. 1. Synthesis and biological activities of the labeling peptides

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Abstract
The synthesis and biological activities of analogs of the peptide hormone angiotensin II (AT) for use in photoaffinity labeling and receptor isolation were described. In the modified sequence of AT,Sar-Arg-Val-Tyr-Val-His-Pro-Phe, the aromatic residues Tyr and Phe were singly or simultaneously replaced by L-4''-nitrophenylalanine, L-4''-amino-3'',5''-diiodophenylalanine, L-4''-aminophenylalanine, L-4''-diazoniumphenylalanine, and L-4''-azido-phenylalanine. The peptides were assembled by solid-phase synthesis and the functional groups in position 4 and/or 8 chemically modified. Radioactivity was introduced by catalytic tritiation of the iodinated peptides to form the photolabeling precursors containing L-4''-amino-3'',5''-diiodophenylalanine. On rabbit aorta the AT analogs substituted in position 4 showed poor affinities (0-15%), in position 8 high relative affinities (16-118%) and in position 4 and 8 additive effects of simultaneous substitutions. The new Boc [Tert butyloxycarbonyl] derivative of L-4''-amino-3'',5''-diiodophenylalanine can be used in peptide synthesis without side-chain protection.

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