Constrained H-Phe-Phe-NH2 analogues with high affinity to the substance P 1-7 binding site and with improved metabolic stability and cell permeability.

@article{Fransson2013ConstrainedHA,
  title={Constrained H-Phe-Phe-NH2 analogues with high affinity to the substance P 1-7 binding site and with improved metabolic stability and cell permeability.},
  author={Rebecca Fransson and Christian Sk{\"o}ld and Jadel Muller Kratz and Richard Berntsson Svensson and Per Artursson and Fred J Nyberg and Mathias Hallberg and Anja Sandstr{\"o}m},
  journal={Journal of medicinal chemistry},
  year={2013},
  volume={56 12},
  pages={4953-65}
}
We recently reported the discovery of H-Phe-Phe-NH2 as a small and high affinity ligand for the substance P 1-7 (SP(1-7), H-Arg-Pro-Lys-Pro-Gln-Gln-Phe-OH) specific binding site and its intriguing ability to reduce neuropathic pain. With the overall aim to develop stable and orally bioavailable SP(1-7) mimetics, the dipeptide was chosen as a lead compound. Herein the structure-activity relationship (SAR) of a set of modified H-Phe-Phe-NH2 analogues is presented together with their potential… CONTINUE READING