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Linear Angiotensin IV Analogues and Incorporation of Unnatural Amino Acids After systematic structure activity studies (SAR) of Ang IV analogues, involving glycine and D-amino acid scans in combination with displacement and incorporation of various alternative amino acid residues it became clear that the N-terminal Val-Tyr-Ile residues of the peptide ligands were important for high affinity to the specific binding site identified (Sardinia et al., 1993), named the AT4 receptor ( 2 ) combined with an unsubstituted amino group in the N-terminal seemed optimal

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