Abstract
Cyclo[Gln-Trp-Phe-Gly-Leu-Met] ( 1) is a selective peptide antagonist of NK-2 receptors. The conformational analysis of this peptide was conducted using nuclear magnetic resonance (NMR) and molecular dynamics. This study improves understanding of the neurokinin ligand—receptor interactions. Two-dimensional Homonuclear Hartmann—Hahn (2D-HOHAHA) and rotating frame Overhauser enhancement spectroscopy (2D-ROESY) were used to assign all the protons and to obtain through-space proton—proton interactions. ROE (rotating frame Overhauser enhancement) constraints molecular dynamics were done to find the conformation which is consistent with the NMR data. Two βI (or βV′) turns around Trp-2-Phe-3 and around Leu-5-Met-6 are found in this peptide which are represented by models. The conformation of this peptide is also compared with the non-peptide NK-2 antagonist SR-48968 ( 2).
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