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A study of aspartyl proteases using intramolecularly quenched fluorogenic peptide substrates

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Abstract

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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Abbreviations

Abz:

2-aminobenzoic acid

Ded:

2,4-dinitrophenylethylenediamine

pNa:

p-nitroaniline

Dnp:

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

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Authors and Affiliations

  1. Chemical faculty, Vorob’evy gory, Moscow State University, 119899, Moscow, Russia

    I. Yu. Filippova, E. N. Lysogorskaya, G. I. Lavrenova, E. S. Oksenoit, L. I. Suvorov & V. V. Starovoitova

Authors
  1. I. Yu. Filippova
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  2. E. N. Lysogorskaya
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  3. G. I. Lavrenova
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  4. E. S. Oksenoit
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  5. L. I. Suvorov
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  6. V. V. Starovoitova
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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). https://doi.org/10.1007/BF02786342

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  • DOI: https://doi.org/10.1007/BF02786342

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