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A study of aspartyl proteases using intramolecularly quenched fluorogenic peptide substrates


A series of fluorogenic tetra-, penta-, and hexapeptide substrates of the general structure Abz-X-Phe-Phe-Y-Ded or (-pNa in place of -Ded), where X=Ala, Ala-Ala, or Val-Ala and Y=−, Ala, or Ala-Ala, were proposed. Kinetic parameters of hydrolysis of these substrates by pepsin, cathepsin D, human gastricsin, pig pepsin, calf chymosin, and aspergillopepsin A were determined. The compounds synthesized proved to be effective substrates for aspartyl proteases of diverse origins.

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2-aminobenzoic acid






2,4-dinitrophenyl. All amino acids areL-enantiomers


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Correspondence to I. Yu. Filippova.

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Filippova, I.Y., Lysogorskaya, E.N., Lavrenova, G.I. et al. A study of aspartyl proteases using intramolecularly quenched fluorogenic peptide substrates. Russ J Bioorg Chem 26, 169–173 (2000).

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Key words

  • aspartyl proteases
  • fluorogenic peptide substrates