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Chemical Compound Review

Cfp-aaf-pab     4-[[(1S)-1-[[(2S)-2-[[(2S)-2- [(1-carboxy-3...

Synonyms: AC1NX8L0, 116560-97-5
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High impact information on Cfp-aaf-pab

  • N-[1-(R,S)-carboxyl-3-phenylpropyl]-Ala-Ala-Phe-p-aminobenzoate (cFP-AAF-pAB), an active-site-directed inhibitor of metalloendopeptidase-24.15, has been shown to lower blood pressure, increase cardiac output and renal blood flow, and potentiate the intravenous bradykinin-induced vasodepressor response [1].
  • The degradation of LHRH and the formation of the N-terminal tri- and pentapeptides was blocked by N-[1-(R,S)-carboxy-3-phenylpropyl]-Ala-Ala-Phe-p-aminobenzoate (cFP-AAF-pAB), a specific, active site directed inhibitor of endopeptidase-24.15 [2].
  • In vivo, when LHRH was injected directly into the third ventricle of rats, the presence of cFP-AAF-pAB inhibited LHRH degradation [2].
  • Similarly to rabbit brain endooligopeptidase A, the PC12 endooligopeptidase A-like activity was enhanced by DTT, totally inhibited by DTNB and 1-10 Phenanthroline, partially inhibited by cFP-AAF-pAb, and not affected by PMSF [3].
  • In addition, BooKase was partially inhibited by cFP-AAF-pAB, a specific inhibitor of thimet oligopeptidase [4].


  1. Effects of a metalloendopeptidase-24.15. Inhibitor on renal hemodynamics and function in rats. Yang, X.P., Saitoh, S., Scicli, A.G., Mascha, E., Orlowski, M., Carretero, O.A. Hypertension (1994) [Pubmed]
  2. Endopeptidase-24.15 is the primary enzyme that degrades luteinizing hormone releasing hormone both in vitro and in vivo. Molineaux, C.J., Lasdun, A., Michaud, C., Orlowski, M. J. Neurochem. (1988) [Pubmed]
  3. Characterization of an endooligopeptidase A-like protein in PC12 cells: activity modulation by cAMP but not by basic fibroblast growth factor. Ferro, E.S., Tambourgy, D.V., Abreu, P.A., Camargo, A.C., Raw, I., Ho, P.L. J. Cell. Biochem. (1995) [Pubmed]
  4. Cattle tick Boophilus microplus salivary gland contains a thiol-activated metalloendopeptidase displaying kininase activity. Bastiani, M., Hillebrand, S., Horn, F., Kist, T.B., Guimarães, J.A., Termignoni, C. Insect Biochem. Mol. Biol. (2002) [Pubmed]
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