The conformations of three endothelin antagonists, a cyclic pentapeptide, a linear tripeptide and a linear hexapeptide, are compared by 'H NMR and molecular dynamics. The three analogues have a Leu and a ~Trp side chain which are oriented parallel, and an acidic group next to the ~Trp residue.

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A comparative conformational analysis of two short pseudopeptides with ETB receptor affinity has been performed by molecular modelling and NMR techniques. This analysis aimed to get insight into probable biorelevant conformations and pharmacophoric patterns necessary for an efficient interaction with the receptor. Thus, it was shown that the two compounds can adopt y-turn (or y-turn-like) conformations, based on which the synthesis of particular, more rigid analogs might be proposed. The results obtained should prove valuable in a strategy aiming to design new endothelin antagonists following a peptide to non-peptide approach.

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