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Design of Sensitive Fluorogenic Substrates For Human Cathepsin D

  1. Author:
    Gulnik, S. V.
    Suvorov, L. I.
    Majer, P.
    Collins, J.
    Kane, B. P.
    Johnson, D. G.
    Erickson, J. W.

  2. Author Address

    Gulnik SV NCI FREDERICK CANC RES & DEV CTR SAIC FREDERICK STRUCT BIOCHEM PROGRAM BLDG 322 POB B FREDERICK, MD 21702 USA NCI FREDERICK CANC RES & DEV CTR SAIC FREDERICK AIDS VACCINE PROGRAM FREDERICK, MD 21702 USA
    1. Year: 1997
  2. Journal: Febs Letters
    1. 413
    2. 2
    3. Pages: 379-384
  4. Type of Article: Article
  1. Abstract:

    Cathepsin D is a lysosomal aspartic proteinase that has been implicated in several pathological processes such as breast cancer and Alzheimer's disease, We designed and synthesized a number of quenched fluorogenic substrates with P2 variations in the series AcEE(EDANS)KPIXFFRLGK(DABCYL)E-NH2, where X=cysteine, methylcysteine, ethylcysteine, tert-butylcysteine, carboxymethylcysteine, methionine, valine or isoleucine, Most of the fluorogenic substrates exhibited greater k(cat)/K-m ratios than the best cathepsin D substrates described so far, Differences in kinetic constants, which were rationalized using structure-based modeling, might make certain substrates useful for particular applications, such as active site titrations or initial velocity determination using a fluorescent plate reader, (C) 1997 Federation of European Biochemical Societies. [References: 25]

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