Synthesis and conformational analysis of cyclic pentapeptide endothelin antagonists

Int J Pept Protein Res. 1996 Sep;48(3):229-39. doi: 10.1111/j.1399-3011.1996.tb00836.x.

Abstract

Two endothelin antagonists cyclo(D-Leu-D-Val-Pro-D-Asp-Trp) (IPI-147), and cyclo (D-Trp-D-Asp-Ac3c-D-Val-Leu) (IPI-725) have been synthetized. Their solution conformations have been studied in aqueous solution by NMR spectroscopy and dynamics simulation. Activity studies show that IPI-725 is a strong ETA antagonist, while IPI-147 is a weak ETA antagonist. Comparison of the solution conformations of these two ETA antagonists suggests that the difference in their activities results from their structural differences. IPI-147 contains a type II beta-turn with a hydrogen bond between NH of D-Val and the C = O of D-Asp. IPI-725, on the other hand, contains two turns, a type II beta-turn with a hydrogen bond between NH of D-Asp and C = O of D-Val, as well as a gamma'-turn with a hydrogen bond formed between D-Val NH and D-Asp carbonyl group. Therefore IPI-147 appears to be more flexible than IPI-725. Although both beta-turns contain the same residues, their orders in the turn are reversed. The beta-turn in IPI-725 is formed with D-Val:Leu:D-Trp:D-Asp, while in IPI-147, the beta-turn is formed with D-Asp:Trp:D-Leu:D-Val. The activities and solution conformations of IPI-147 and IPI-725 were also compared with BQ-123 [cyclo(D-Trp-D-Asp-Pro-D-Val-Leu)], a well characterized, highly potent endothelin antagonist.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Endothelins / antagonists & inhibitors*
  • Molecular Structure
  • Oligopeptides / chemical synthesis
  • Oligopeptides / chemistry*
  • Oligopeptides / pharmacology
  • Peptides, Cyclic / chemical synthesis*
  • Peptides, Cyclic / chemistry*
  • Peptides, Cyclic / pharmacology*

Substances

  • Endothelins
  • Oligopeptides
  • Peptides, Cyclic
  • cyclo(leucyl-valyl-prolyl-aspartyl-tryptophan)
  • cyclo(tryptophyl-aspartyl-acetyl(3)c-valyl-leucyl)