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  • Title: A structure-activity study of a C-terminal endothelin analogue.
    Author: Cassano E, Galoppini C, Giusti L, Hamdan M, Macchia M, Mazzoni MR, Menchini E, Pegoraro S, Rovero P.
    Journal: Folia Biol (Praha); 1998; 44(1):11-4. PubMed ID: 10730869.
    Abstract:
    We report a structure-activity study of an endothelin (ET) analogue, obtained by introduction of a non-aminoacidic portion on the C-terminal ET pentapeptide. The peptidic moiety was modified with systematic replacement of each residue by alanine (Ala scan); further modifications were performed at the C-terminus. The biological activity was analyzed at both ET(A) and ET(B) receptor subtypes, showing that the two C-terminal residues (Ile-Trp) are very important for the activity. On the contrary, the aminoacidic central portion of the molecule appears to be much more tolerant toward modifications.
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