| Autor: |
Lukaszuk, Aneta, Demaegdt, Heidi, Van Den Eynde, Isabelle, Vanderheyden, Patrick, Vauquelin, Georges, Tourwe, Dirk |
| Přispěvatelé: |
Faculty of Sciences and Bioengineering Sciences, Chemistry, Department of Bio-engineering Sciences, Experimental Pharmacology, Molecular and Biochemical Pharmacology, Organic Chemistry |
| Jazyk: |
angličtina |
| Rok vydání: |
2011 |
| Předmět: |
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| Popis: |
The aromatic amino acids Tyr and Phe in angiotensin IV (Ang IV) were conformationally constrained by the use of β-Me substituted analogs, or cyclic constrained analogs. None of these modifications was allowed for Tyr¹, while only e-β-MePhe⁶ substitution resulted in an AngIV analog with high IRAP potency and selectivity versus AP-N or the AT₁ receptor. This indicates an important role of the orientation of the Phe⁶ for inducing selectivity. Pro⁵ replacement with 2-aminocyclopentanecarboxylic acid maintained IRAP potency and abolished AT₁ affinity. These results confirm the importance of conformational constrained amino acids to generate selectivity in bioactive peptides. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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