Document 0872
 DOCN  M9470872
 TI    Inhibition of activity of the protease from bovine leukemia virus.
 DT    9409
 AU    Menard A; Leonard R; Llido S; Geoffre S; Picard P; Berteau F; Precigoux
       G; Hospital M; Guillemain B; INSERM Unite 328, fondation Bergonie,
       Bordeaux, France.
 SO    FEBS Lett. 1994 Jun 13;346(2-3):268-72. Unique Identifier : AIDSLINE
       MED/94283610
 AB    In view of the close similarity between bovine leukemia virus (BLV) and
       human T-cell leukemia virus type I (HTLV-I) we investigated the
       possibility of developing specific inhibitors of the proteases of these
       retroviruses using the purified enzyme from BLV. We tested the ability
       of this protease to specifically cleave various short oligopeptide
       substrates containing cleavage sites of BLV and HTLV-I proteases, as
       well as a recombinant BLV Gag precursor. The best substrate, a synthetic
       decapeptide bearing the natural cleavage site between the matrix and the
       capsid proteins of BLV Gag precursor polyprotein, was used to develop an
       inhibition assay. We determined the relative inhibitory effect of
       synthetic Gag precursor-like peptides in which the cleavable site was
       replaced by a non-hydrolyzable moiety. The encouraging inhibitory effect
       of these compounds indicates that potent non-peptidic inhibitors for
       retroviral proteases are not unattainable.
 DE    Amino Acid Sequence  Binding Sites  Chromatography, High Pressure Liquid
       Drug Design  Gene Products, gag/CHEMISTRY/METABOLISM  HTLV-I/ENZYMOLOGY
       Leukemia Virus, Bovine/*ENZYMOLOGY  Molecular Sequence Data
       Oligopeptides/CHEMISTRY/METABOLISM/PHARMACOLOGY  Pepstatins/PHARMACOLOGY
       Peptide Peptidohydrolases/CHEMISTRY/*METABOLISM  Protease
       Inhibitors/CHEMISTRY/*PHARMACOLOGY  Protein Precursors/METABOLISM
       Recombinant Proteins/METABOLISM  Substrate Specificity  Support,
       Non-U.S. Gov't  JOURNAL ARTICLE

       SOURCE: National Library of Medicine.  NOTICE: This material may be
       protected by Copyright Law (Title 17, U.S.Code).