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  • acyl migration-type prodrug  (2)
  • 31P-NMR  (1)
  • Springer  (3)
  • 1995-1999  (3)
  • 1965-1969
  • 1960-1964
  • 1935-1939
  • 1920-1924
  • 1999  (3)
  • 1
    ISSN: 1573-5176
    Keywords: Chattonella antiqua ; diel verticalmigration ; intracellular phosphate ; large axenicculture tank ; 31P-NMR ; phosphate accumulation ; Raphidophyceae ; salinity and nutrient stratification
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The ecological advantage of diel vertical migration on the nutrition and accumulation of Chattonella antiqua, which is one of the dominant red-tide forming phytoplankton species in the Seto Inland Sea of Japan, was examined using a large axenic culture tank, in which vertical stratification of salinity, temperature and nutrients was maintained, analogous to natural conditions observed when red tides occur. C. antiqua was capable of migrating through very sharp salinity and temperature gradients. At night the species migrated to the deep nutrient-rich water and assimilated nutrients. During the daytime it migrated to the nutrient-depleted surface water and used the accumulated nutrients for photosynthesis. Nitrogen uptake was synchronized with phosphate uptake. 31P-NMR spectroscopy during the migration experiment revealed that C. antiqua has the capability of nocturnal phosphate uptake in the deep nutrient-rich water, but no capability of synthesizing polyphosphate, which was considered to be the intracellular phosphate pool. These findings were compared with those reported for another raphidophycean, Heterosigma akashiwo. Although both species carry out vertical migration and nocturnal nutrient uptake, only H. akashiwo has the capability of making an intracellular polyphosphate pool.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    International journal of peptide research and therapeutics 6 (1999), S. 275-281 
    ISSN: 1573-3904
    Keywords: acyl migration-type prodrug ; anti-HIV drug ; conjugate of HIV protease inhibitor with RT inhibitor ; HIV protease inhibitor ; KNI compound ; substrate transition state analog
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The human immunodeficiency virus (HIV) contains an aspartic protease known to be essential for retroviral maturation and replication. Based on the transition state for substrate processing, we designed and synthesized a novel class of HIV-1 protease inhibitors containing an unnatural amino acid, allophenylnorstatine (i.e. (2S,3S)-3-amino-2-hydroxy-4-phenylbutyric acid), with a hydroxymethylcarbonyl (HMC) isostere. The stereochemistry of the hydroxyl group was important for enzyme inhibition and the HMC group interacted efficiently with the aspartic acid carboxyl groups of the HIV-1 protease active site in essentially the same hydrogen bonding mode as the transition state. Small dipeptide-based HIV-1 protease inhibitors containing the HMC isostere were studied. Since some of these inhibitors showed low solubility in water, we designed a novel class of 'O→N intramolecular acyl migration'-type prodrugs of HIV-1 protease inhibitors for solubilization. Furthermore, we designed and synthesized a novel prodrug-type anti-HIV agent – the conjugate of a peptidomimetic HIV-1 protease inhibitor containing a free carboxylic acid with a nucleoside reverse transcriptase inhibitor. These studies may be useful in anti-HIV drug development.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    International journal of peptide research and therapeutics 6 (1999), S. 275-281 
    ISSN: 1573-3904
    Keywords: acyl migration-type prodrug ; anti-HIV drug ; conjugate of HIV protease inhibitor with RT inhibitor ; HIV protease inhibitor ; KNI compound ; substrate transition state analog
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Summary The human immunodeficiency virus (HIV) contains an aspartic protease known to be essential for retroviral maturation and replication. Based on the transition state for substrate processing, we designed and synthesized a novel class of HIV-1 protease inhibitors containing an unnatural amino acid, allophenylnorstatine (i.e. (2S, 3S)-3-amino-2-hydroxy-4-phenylbutyric acid), with a hydroxymethylcarbonyl (HMC) isostere. The stereochemistry of the hydroxyl group was important for enzyme inhibition and the HMC group interacted efficiently with the aspartic acid carboxyl groups of the HIV-1 protease active site in essentially the same hydrogen bonding mode as the transition state. Small dipeptide-based HIV-1 protease inhibitors containing the HMC isostere were studied. Since some of these inhibitors showed low solubility in water, we designed a novel class of ‘O→N intramolecular acyl migration’-type prodrugs of HIV-1 protease inhibitors for solubilization. Furthermore, we designed and synthesized a novel prodrug-type anti-HIV agent — the conjugate of a peptidomimetic HIV-1 protease inhibitor containing a free carboxylic acid with a nucleoside reverse transcriptase inhibitor. These studies may be useful in anti-HIV drug development.
    Type of Medium: Electronic Resource
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