A study of aspartyl proteases using intramolecularly quenched fluorogenic peptide substrates

A series of fluorogenic tetra-, penta-, and hexapeptide substrates of the g eneral 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 determi ned. The compounds synthesized proved to be effective substrates for aspart yl proteases of diverse origins.