Conformational study of cyclo[D‐Trp‐D‐Asp‐Pro‐D‐Val‐Leu], an endothelin‐A receptor‐selective antagonist

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Abstract
The conformation of cyclo[D‐Trp‐D‐Asp‐Pro‐D‐Val‐Leu], (BQ123), an endothelin‐A receptor‐selective antagonist, has been studied in 20% acetonitrile in water by CD and NMR spectroscopy. CD studies showed the peptide adopted a similar, constrained conformation in both water alone and 20% acetonitrile in water. NMR spectra showed the proline residue to be in the trans conformation and 2 of the NH protons to exchange slowly with the solvent, indicating hydrogen bonding. Structural constraints derived from the NMR spectra were used to define the conformation in molecular dynamics simulations. A single backbone conformation is observed for the cycle, comprising a β type II turn and a γ′ turn.

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