Development and characterization of novel potent and stable inhibitors of endopeptidase EC 3.4.24.15.

@article{Shrimpton2000DevelopmentAC,
  title={Development and characterization of novel potent and stable inhibitors of endopeptidase EC 3.4.24.15.},
  author={Corie N. Shrimpton and Giovanni Abbenante and Rebecca A. Lew and Isabel Helen Smith},
  journal={The Biochemical journal},
  year={2000},
  volume={345 Pt 2},
  pages={
          351-6
        }
}
Solid-phase synthesis was used to prepare a series of modifications to the selective and potent inhibitor of endopeptidase EC 3.4.24.15 (EP24.15), N-[1(R, S)-carboxy-3-phenylpropyl]-Ala-Ala-Tyr-p-aminobenzoate (cFP), which is degraded at the Ala-Tyr bond, thus severely limiting its utility in vivo. Reducing the amide bond between the Ala and Tyr decreased the potency of the inhibitor to 1/1000. However, the replacement of the second alanine residue immediately adjacent to the tyrosine with… CONTINUE READING
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Endopeptidases 3.4.24.15 and 24.16 in endothelial cells: potential role in vasoactive peptide metabolism.

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