An NMR, CD, molecular dynamics, and fluorometric study of the conformation of the bradykinin antagonist B-9340 in water and in aqueous micellar solutions.

  title={An NMR, CD, molecular dynamics, and fluorometric study of the conformation of the bradykinin antagonist B-9340 in water and in aqueous micellar solutions.},
  author={Jan Sejbal and John R. Cann and John M Stewart and Lajos Gera and George Kotovych},
  journal={Journal of medicinal chemistry},
  volume={39 6},
A detailed NMR, CD, fluorometry, and molecular modeling study of a novel bradykinin antagonist B-9340, containing a novel amino acid D-Igl (alpha-(2-indanyl)glycine) at position 7, was carried out. The sequence of B-9340 is D-Arg0-Arg1-Pro2-Hyp3-Gly4-Thi5-Ser6-D- Igl7-Oic8-Arg9, where Hyp is hydroxyproline, Thi is beta-(2-thienyl)alanine, and Oic is (3aS,7aS)-octahydroindole-2-carboxylic acid. The CD results exhibit a striking effect of SDS on the spectrum of the BK antagonist, indicating that… Expand
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An isotope-edited NMR study of the peptide hormone bradykinin bound to the Fab fragment of a monoclonal antibody against bradykinsin (MBK3) is reported, indicating that essentially the entire nonapeptide is involved in binding. Expand
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Addition of Tyr at the N-terminal to bradykinin preserves its overall conformation
Summary Bradykinin, Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg (BK), possesses diverse pharmacological activity. Addition of Tyr to the N-terminal of BK (Tyr-BK) retains 90% of the activity. TheExpand
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The preferred conformation of Proadrenomedullin N‐Terminal 20 Peptide (PAMP; ARLDVASEFRKKWNKWALSR‐amide) has been determined using 1H and 13C two‐dimensional nuclear magnetic resonance (NMR) spectroscopy and molecular modeling, and it is postulated that the polar charged residues Arg2, Lys12, and Arg20 are responsible for the initial interaction of the peptide with the micelle. Expand
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