Abstract
The molecular conformations of dermorphin, Try1-D-Ala2 - Phe3 - Gly4 - Tyr5 - Pro6 - Ser7-NH2, are derived from FT-IR, Raman, CD, and 2D NMR spectroscopic studies in aqueous solution. Segawa et al. (1994,1995) have recently reported NMR studies of dermorphin in aqueous solution from which a folded conformation has been postulated. The folded conformation of dermorphin suggested by this study is characterized by a stacking of the aromatic side chains of Try1 and Phe3. This appears to be critical to the pharmacological profile of dermorphin. The experimentally derived conformation bears partial resemblance to the low energy conformations predicted by molecular mechanics calculations. The proposed conformational model and its possible relevance to the μ-agonist activity of dermorphin are discussed.
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