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

1978 ◽  
Vol 21 (9) ◽  
pp. 860-864 ◽  
Author(s):  
Emanuel H. F. Escher ◽  
Nguyen Thi Mai Dung ◽  
Helene Robert ◽  
Domenico C. Regoli ◽  
Serge A. St. Pierre
Keyword(s):  
Angiotensin Ii ◽  
Biological Activities ◽  
Photoaffinity Labeling ◽  
Angiotensin Ii Receptor

ChemInform Abstract: PHOTOAFFINITY LABELING OF THE ANGIOTENSIN II RECEPTOR. PART 1. SYNTHESIS AND BIOLOGICAL ACTIVITIES OF THE LABELING PEPTIDES

1979 ◽  
Vol 10 (8) ◽  
Author(s):  
E. H. F. ESCHER ◽  
THI MAI DUNG NGUYEN THI MAI DUNG NGUYEN ◽  
H. ROBERT ◽  
S. A. ST-PIERRE ◽  
D. C. REGOLI
Keyword(s):  
Angiotensin Ii ◽  
Biological Activities ◽  
Photoaffinity Labeling ◽  
Angiotensin Ii Receptor

Photoaffinity labeling of the angiotensin II receptor; pharmacology of the labeling peptides in the dark

1978 ◽  
Vol 56 (6) ◽  
pp. 956-962 ◽  
Author(s):  
E. Escher ◽  
T. M. D. Nguyen ◽  
D. Regoli
Keyword(s):  
Angiotensin Ii ◽  
Biological Activities ◽  
Photoaffinity Labeling ◽  
Rabbit Aorta ◽  
Competitive Inhibitor ◽  
Current View ◽  
Angiotensin Ii Receptor ◽  
Aromatic Side Chain ◽  
Receptor Pharmacology ◽  
Measurable Activity

The biological activities of photoaffinity labeling analogs of angiotensin II (ATII) and their precursors were measured in rabbit aorta strips in the dark. Most of the analogs behave as reversible, specific agonists, one as a competitive inhibitor. The activities are discussed in line with the current view of structural requirements. The modifications consisted of substitutions on the aromatic nuclei of Tyr4 and Phe8 in [Sar1]ATII with (4′-NO2)Phe, (4′-NH2)Phe, (4′-N3)Phe, (4′-N2+)Phe, and (4′-NH2-3′, 5′-I2)Phe. It is shown that the affinity of the ATII analogs modified in position 4 depends on the electronegativity and not on space-filling properties of the aromatic residue; rising electronegativity lowers the affinity, i.e., [Sar1, (4′-NO2)Phe4]ATII has no more measurable activity. Substituting the aromatic side chain in position 8 of [Sar1]ATII gives well-binding analogs with intrinsic activities from 0 to 100% and activity seems to depend only on stereochemical requirements. Agonists and partial agonists bear rather small groups like -NH2, -N3, -NO2, and -N2+. The only antagonist [Sar1, (4′-NH2-3′,5′-I2)Phe8]ATII resembles the antagonist [Sar1, Leu8]ATII in competitivity and binding.

Design, Synthesis, and Biological Activities of Four Angiotensin II Receptor Ligands with γ-Turn Mimetics Replacing Amino Acid Residues 3−5

1997 ◽  
Vol 40 (6) ◽  
pp. 903-919 ◽  
Author(s):  
Boris Schmidt ◽  
Susanna Lindman ◽  
Weimin Tong ◽  
Gunnar Lindeberg ◽  
Adolf Gogoll ◽  
...  
Keyword(s):  
Amino Acid ◽  
Angiotensin Ii ◽  
Biological Activities ◽  
Amino Acid Residues ◽  
Angiotensin Ii Receptor ◽  
Receptor Ligands ◽  
Design Synthesis
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