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  • KNI compound  (2)
  • KR-ET-1  (2)
  • Springer  (4)
  • 1995-1999  (4)
  • 1960-1964
  • 1935-1939
  • 1920-1924
Collection
Keywords
Publisher
  • Springer  (4)
Years
  • 1995-1999  (4)
  • 1960-1964
  • 1935-1939
  • 1920-1924
Year
  • 1
    Electronic Resource
    Electronic Resource
    Improvement in the oxidative folding of endothelin-1 by a Lys-Arg extension at the amino terminus: Implication of a salt bridge between Arg-1 and Asp8 (1997)
    Springer
    International journal of peptide research and therapeutics 4 (1997), S. 185-192 
    Details
    ISSN: 1573-3904
    Keywords: α-Helix ; Carboxamide substitution ; Circular dichroism ; Disulfide isomer ; KR-ET-1 ; Prosequence
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract An amino-terminal extension of endothelin-1 by the Lys-Arg dipeptide in the prosequence (KR-ET-1) greatly increased the ratio of native-type to non-native-type disulfide isomer (96/4 versus 71/29) during the oxidative folding reaction. This improvement was completely abolished by substituting Asn for Asp at position 8 (D8N-KR-ET-1), whereas most of it was maintained with similar carboxamide analogues replaced at Glu10 or Asp18. Structure analyses by circular dichroism spectroscopy revealed that (i) in the carboxylate state, the α-helical content of the native-type isomer of KR-ET-1 is higher than that of the native-type isomer of ET-1, while such a variation is not observed in the corresponding non-native-type isomer of KR-ET-1; and (ii) the enhanced α-helicity resulting from the Lys-Arg extension is largely diminished in D8N-KR-ET-1. From these results and our previous findings that the helical structure in KR-ET-1 is stabilized by a particular salt bridge between the extended Arg-1 basic moiety and either the Asp8 or Glu10 acidic side chain in ET-1 [Aumelas, A. et al., Biochemistry, 34 (1995) 4546], we conclude that the formation of a specific salt bridge between the side chains of Arg-1 and Asp8 in KR-ET-1 is critical for the predominant generation of the native-type disulfide isomer, probably because it stabilizes the helical structure of parental ET-1.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1008835323518
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  • 2
    Electronic Resource
    Electronic Resource
    Design of small peptidomimetic HIV-1 protease inhibitors and prodrug forms (1999)
    Springer
    International journal of peptide research and therapeutics 6 (1999), S. 275-281 
    Details
    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
    URL: http://dx.doi.org/10.1023/A:1008944023236
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  • 3
    Electronic Resource
    Electronic Resource
    Design of small peptidomimetic HIV-1 protease inhibitors and prodrug forms (1999)
    Springer
    International journal of peptide research and therapeutics 6 (1999), S. 275-281 
    Details
    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
    URL: http://dx.doi.org/10.1007/BF02443422
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    Paper (German National Licenses)
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  • 4
    Electronic Resource
    Electronic Resource
    Improvement in the oxidative folding of endothelin-1 by a lys-Arg extension at the amino terminus: Implication of a salt bridge between Arg−1 and Asp8 (1997)
    Springer
    International journal of peptide research and therapeutics 4 (1997), S. 185-192 
    Details
    ISSN: 1573-3904
    Keywords: α-Helix ; Carboxamide substitution ; Circular dichroism ; Disulfide isomer ; KR-ET-1 ; Prosequence
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Summary An amino-terminal extension of endothelin-l by the lys-Arg dipeptide in the prosequence (KR-ET-1) greatly increased the ratio of native-type to non-native-type disulfide isomer (96/4 versus 71/29) during the oxidative folding reaction. This improvement was completely abolished by substituting Asn for Asp at position 8 (D8N-KR-ET-1), whereas most of it was maintained with similar carboxamide analogues replaced at Glu10 or Asp18. Structure analyses by circular dichroism spectroscopy revealed that (i) in the carboxylate state, the α-helical content of the native-type isomer of KR-ET-l is higher than that of the native-type isomer of ET-1, while such a variation is not observed in the corresponding non-native-type isomer of KR-ET-l; and (ii) the enhanced α-helicity resulting from the Lys-Arg extension is largely diminished in D8N-KR-ET-l. From these results and our previous findings that the helical structure in KR-ET-l is stabilized by a particular salt bridge between the extended Arg−1 basic moiety and either the Asp8 or Glu10 acidic side chain in Et-1 [Aumelas, A. et al., Biochemistry, 34 (1995) 4546], we conclude that the formation of a specific salt bridge between the side chains of Arg−1 and Asp8 in KR-ET-1 is critical for the predominant generation of the native-type disulfide isomer, probably because it stabilizes the helical structure of parental ET-1.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02443532
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    Paper (German National Licenses)
    Fulltext
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