Selective inhibition of fibroblast activation protein protease based on dipeptide substrate specificity.

@article{Edosada2006SelectiveIO,
  title={Selective inhibition of fibroblast activation protein protease based on dipeptide substrate specificity.},
  author={Conrad Yap Edosada and Clifford L Quan and Christian Wiesmann and Thuy H Tran and Dan Sutherlin and Mark Reynolds and James Michael Elliott and Helga E Raab and Wayne J. Fairbrother and Beni B. Wolf},
  journal={The Journal of biological chemistry},
  year={2006},
  volume={281 11},
  pages={7437-44}
}
Fibroblast activation protein (FAP) is a transmembrane serine peptidase that belongs to the prolyl peptidase family. FAP has been implicated in cancer; however, its specific role remains elusive because inhibitors that distinguish FAP from other prolyl peptidases like dipeptidyl peptidase-4 (DPP-4) have not been developed. To identify peptide motifs for FAP-selective inhibitor design, we used P(2)-Pro(1) and acetyl (Ac)-P(2)-Pro(1) dipeptide substrate libraries, where P(2) was varied and… CONTINUE READING

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